eF-site ID 2qji-ABCDEFGHIJKLMNOPQRST PDB Code 2qji Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T Title M. jannaschii ADH synthase complexed with dihydroxyacetone phosphate and glycerol Classification LYASE Compound Putative aldolase MJ0400 Source Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (Y400_METJA) Sequence A:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK B:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK C:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK D:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK E:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK F:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK G:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK H:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK I:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK J:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK K:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK L:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK M:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK N:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK O:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK P:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK Q:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK R:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK S:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIF QHDDVVGITRAVCKIVHENADVEEALKEIRK T:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVG LIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVN VGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQN ERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGC PAPVVVAGGPKTDEEFLQMIKDAMEAGAAGVAVGRNIFQH DDVVGITRAVCKIVHENADVEEALKEIRK Description (1)  Putative aldolase MJ0400 (E.C.4.2.1.-) Functional site 1) chain A residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 2) chain A residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 3) chain A residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 4) chain A residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 5) chain A residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 6) chain A residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 7) chain A residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 8) chain A residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 9) chain A residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 10) chain A residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 11) chain B residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 12) chain B residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 13) chain B residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 14) chain B residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 15) chain B residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 16) chain B residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 17) chain B residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 18) chain B residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 19) chain B residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 20) chain B residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 21) chain C residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 22) chain C residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 23) chain C residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 24) chain C residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 25) chain C residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 26) chain C residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 27) chain C residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 28) chain C residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 29) chain C residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 30) chain C residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 31) chain D residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 32) chain D residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 33) chain D residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 34) chain D residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 35) chain D residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 36) chain D residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 37) chain D residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 38) chain D residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 39) chain D residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 40) chain D residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 41) chain E residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 42) chain E residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 43) chain E residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 44) chain E residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 45) chain E residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 46) chain E residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 47) chain E residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 48) chain E residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 49) chain E residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 50) chain E residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 51) chain F residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 52) chain F residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 53) chain F residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 54) chain F residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 55) chain F residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 56) chain F residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 57) chain F residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 58) chain F residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 59) chain F residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 60) chain F residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 61) chain G residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 62) chain G residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 63) chain G residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 64) chain G residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 65) chain G residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 66) chain G residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 67) chain G residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 68) chain G residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 69) chain G residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 70) chain G residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 71) chain H residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 72) chain H residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 73) chain H residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 74) chain H residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 75) chain H residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 76) chain H residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 77) chain H residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 78) chain H residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 79) chain H residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 80) chain H residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 81) chain I residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 82) chain I residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 83) chain I residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 84) chain I residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 85) chain I residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 86) chain I residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 87) chain I residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 88) chain I residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 89) chain I residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 90) chain I residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 91) chain J residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 92) chain J residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 93) chain J residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 94) chain J residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 95) chain J residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 96) chain J residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 97) chain J residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 98) chain J residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 99) chain J residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 100) chain J residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 101) chain K residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 102) chain K residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 103) chain K residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 104) chain K residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 105) chain K residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 106) chain K residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 107) chain K residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 108) chain K residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 109) chain K residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 110) chain K residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 111) chain L residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 112) chain L residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 113) chain L residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 114) chain L residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 115) chain L residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 116) chain L residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 117) chain L residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 118) chain L residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 119) chain L residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 120) chain L residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 121) chain M residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 122) chain M residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 123) chain M residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 124) chain M residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 125) chain M residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 126) chain M residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 127) chain M residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 128) chain M residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 129) chain M residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 130) chain M residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 131) chain N residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 132) chain N residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 133) chain N residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 134) chain N residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 135) chain N residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 136) chain N residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 137) chain N residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 138) chain N residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 139) chain N residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 140) chain N residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 141) chain O residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 142) chain O residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 143) chain O residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 144) chain O residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 145) chain O residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 146) chain O residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 147) chain O residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 148) chain O residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 149) chain O residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 150) chain O residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 151) chain P residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 152) chain P residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 153) chain P residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 154) chain P residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 155) chain P residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 156) chain P residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 157) chain P residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 158) chain P residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 159) chain P residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 160) chain P residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 161) chain Q residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 162) chain Q residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 163) chain Q residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 164) chain Q residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 165) chain Q residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 166) chain Q residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 167) chain Q residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 168) chain Q residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 169) chain Q residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 170) chain Q residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 171) chain R residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 172) chain R residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 173) chain R residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 174) chain R residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 175) chain R residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 176) chain R residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 177) chain R residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 178) chain R residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 179) chain R residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 180) chain R residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 181) chain S residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 182) chain S residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 183) chain S residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 184) chain S residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 185) chain S residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 186) chain S residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 187) chain S residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 188) chain S residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 189) chain S residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 190) chain S residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 191) chain T residue 31 type sequence P description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 192) chain T residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 193) chain T residue 34 type sequence H description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 194) chain T residue 184 type sequence K description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 195) chain T residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 196) chain T residue 210 type sequence G description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 197) chain T residue 235 type sequence A description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 198) chain T residue 236 type sequence V description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 199) chain T residue 237 type sequence G description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 200) chain T residue 238 type sequence R description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 201) chain A residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 202) chain A residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 203) chain A residue 37 type sequence S description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 204) chain A residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 205) chain A residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 206) chain A residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 207) chain A residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 208) chain A residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 209) chain A residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL A 500 source : CC3 210) chain B residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL B 500 source : CC4 211) chain B residue 37 type sequence S description BINDING SITE FOR RESIDUE GOL B 500 source : CC4 212) chain B residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL B 500 source : CC4 213) chain B residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL B 500 source : CC4 214) chain B residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL B 500 source : CC4 215) chain B residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL B 500 source : CC4 216) chain B residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL B 500 source : CC4 217) chain B residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL B 500 source : CC4 218) chain C residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL C 500 source : CC5 219) chain C residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL C 500 source : CC5 220) chain C residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL C 500 source : CC5 221) chain C residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL C 500 source : CC5 222) chain C residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL C 500 source : CC5 223) chain C residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL C 500 source : CC5 224) chain D residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL D 500 source : CC6 225) chain D residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL D 500 source : CC6 226) chain D residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL D 500 source : CC6 227) chain D residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL D 500 source : CC6 228) chain D residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL D 500 source : CC6 229) chain D residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL D 500 source : CC6 230) chain D residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL D 500 source : CC6 231) chain D residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL D 500 source : CC6 232) chain E residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 233) chain E residue 37 type sequence S description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 234) chain E residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 235) chain E residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 236) chain E residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 237) chain E residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 238) chain E residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 239) chain E residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 240) chain E residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL E 500 source : CC7 241) chain F residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 242) chain F residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 243) chain F residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 244) chain F residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 245) chain F residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 246) chain F residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 247) chain F residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 248) chain F residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 249) chain F residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL F 500 source : CC8 250) chain G residue 37 type sequence S description BINDING SITE FOR RESIDUE GOL G 500 source : CC9 251) chain G residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL G 500 source : CC9 252) chain G residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL G 500 source : CC9 253) chain G residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL G 500 source : CC9 254) chain G residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL G 500 source : CC9 255) chain G residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL G 500 source : CC9 256) chain G residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL G 500 source : CC9 257) chain G residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL G 500 source : CC9 258) chain H residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL H 500 source : DC1 259) chain H residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL H 500 source : DC1 260) chain H residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL H 500 source : DC1 261) chain H residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL H 500 source : DC1 262) chain H residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL H 500 source : DC1 263) chain H residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL H 500 source : DC1 264) chain H residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL H 500 source : DC1 265) chain I residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 266) chain I residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 267) chain I residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 268) chain I residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 269) chain I residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 270) chain I residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 271) chain I residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 272) chain I residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 273) chain I residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL I 500 source : DC2 274) chain J residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL J 500 source : DC3 275) chain J residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL J 500 source : DC3 276) chain J residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL J 500 source : DC3 277) chain J residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL J 500 source : DC3 278) chain J residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL J 500 source : DC3 279) chain J residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL J 500 source : DC3 280) chain K residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 281) chain K residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 282) chain K residue 37 type sequence S description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 283) chain K residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 284) chain K residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 285) chain K residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 286) chain K residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 287) chain K residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 288) chain K residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 289) chain K residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL K 500 source : DC4 290) chain L residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL L 500 source : DC5 291) chain L residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL L 500 source : DC5 292) chain L residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL L 500 source : DC5 293) chain L residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL L 500 source : DC5 294) chain L residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL L 500 source : DC5 295) chain L residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL L 500 source : DC5 296) chain L residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL L 500 source : DC5 297) chain M residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 298) chain M residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 299) chain M residue 37 type sequence S description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 300) chain M residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 301) chain M residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 302) chain M residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 303) chain M residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 304) chain M residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 305) chain M residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 306) chain M residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL M 500 source : DC6 307) chain N residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 308) chain N residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 309) chain N residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 310) chain N residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 311) chain N residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 312) chain N residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 313) chain N residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 314) chain N residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 315) chain N residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL N 500 source : DC7 316) chain O residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 317) chain O residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 318) chain O residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 319) chain O residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 320) chain O residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 321) chain O residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 322) chain O residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 323) chain O residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 324) chain O residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL O 500 source : DC8 325) chain P residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL P 500 source : DC9 326) chain P residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL P 500 source : DC9 327) chain P residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL P 500 source : DC9 328) chain P residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL P 500 source : DC9 329) chain P residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL P 500 source : DC9 330) chain P residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL P 500 source : DC9 331) chain Q residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 332) chain Q residue 37 type sequence S description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 333) chain Q residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 334) chain Q residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 335) chain Q residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 336) chain Q residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 337) chain Q residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 338) chain Q residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 339) chain Q residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL Q 500 source : EC1 340) chain R residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 341) chain R residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 342) chain R residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 343) chain R residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 344) chain R residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 345) chain R residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 346) chain R residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 347) chain R residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 348) chain R residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL R 500 source : EC2 349) chain S residue 33 type sequence D description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 350) chain S residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 351) chain S residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 352) chain S residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 353) chain S residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 354) chain S residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 355) chain S residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 356) chain S residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 357) chain S residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL S 500 source : EC3 358) chain T residue 36 type sequence V description BINDING SITE FOR RESIDUE GOL T 500 source : EC4 359) chain T residue 65 type sequence H description BINDING SITE FOR RESIDUE GOL T 500 source : EC4 360) chain T residue 85 type sequence H description BINDING SITE FOR RESIDUE GOL T 500 source : EC4 361) chain T residue 87 type sequence S description BINDING SITE FOR RESIDUE GOL T 500 source : EC4 362) chain T residue 88 type sequence G description BINDING SITE FOR RESIDUE GOL T 500 source : EC4 363) chain T residue 89 type sequence G description BINDING SITE FOR RESIDUE GOL T 500 source : EC4 364) chain T residue 99 type sequence K description BINDING SITE FOR RESIDUE GOL T 500 source : EC4 365) chain T residue 119 type sequence H description BINDING SITE FOR RESIDUE GOL T 500 source : EC4 366) chain A residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 367) chain J residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 368) chain K residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 369) chain L residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 370) chain M residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 371) chain N residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 372) chain O residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 373) chain P residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 374) chain Q residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 375) chain R residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 376) chain S residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 377) chain B residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 378) chain T residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 379) chain C residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 380) chain D residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 381) chain E residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 382) chain F residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 383) chain G residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 384) chain H residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 385) chain I residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 386) chain A residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 387) chain J residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 388) chain K residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 389) chain L residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 390) chain M residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 391) chain N residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 392) chain O residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 393) chain P residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 394) chain Q residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 395) chain R residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 396) chain S residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 397) chain B residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 398) chain T residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 399) chain C residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 400) chain D residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 401) chain E residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 402) chain F residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 403) chain G residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 404) chain H residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 405) chain I residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 406) chain A residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 407) chain J residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 408) chain K residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 409) chain L residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 410) chain M residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 411) chain N residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 412) chain O residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 413) chain P residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 414) chain Q residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 415) chain R residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 416) chain S residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 417) chain B residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 418) chain T residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 419) chain C residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 420) chain D residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 421) chain E residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 422) chain F residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 423) chain G residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 424) chain H residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 425) chain I residue 184 type ACT_SITE sequence K description Schiff-base intermediate with substrate => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI3 426) chain A residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 427) chain C residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 428) chain C residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 429) chain C residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 430) chain D residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 431) chain D residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 432) chain D residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 433) chain D residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 434) chain E residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 435) chain E residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 436) chain E residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 437) chain A residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 438) chain E residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 439) chain F residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 440) chain F residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 441) chain F residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 442) chain F residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 443) chain G residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 444) chain G residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 445) chain G residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 446) chain G residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 447) chain H residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 448) chain A residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 449) chain H residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 450) chain H residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 451) chain H residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 452) chain I residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 453) chain I residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 454) chain I residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 455) chain I residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 456) chain J residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 457) chain J residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 458) chain J residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 459) chain A residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 460) chain J residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 461) chain K residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 462) chain K residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 463) chain K residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 464) chain K residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 465) chain L residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 466) chain L residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 467) chain L residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 468) chain L residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 469) chain M residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 470) chain B residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 471) chain M residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 472) chain M residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 473) chain M residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 474) chain N residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 475) chain N residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 476) chain N residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 477) chain N residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 478) chain O residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 479) chain O residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 480) chain O residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 481) chain B residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 482) chain O residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 483) chain P residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 484) chain P residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 485) chain P residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 486) chain P residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 487) chain Q residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 488) chain Q residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 489) chain Q residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 490) chain Q residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 491) chain R residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 492) chain B residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 493) chain R residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 494) chain R residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 495) chain R residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 496) chain S residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 497) chain S residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 498) chain S residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 499) chain S residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 500) chain T residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 501) chain T residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 502) chain T residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 503) chain B residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 504) chain T residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 505) chain C residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4

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