eF-site ID 2qjh-ABCDEFGHIJKLMNOPQRST PDB Code 2qjh 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 covalently bound to dihydroxyacetone phosphate Classification LYASE Compound Putative aldolase MJ0400 Source null (Y400_METJA) Sequence A:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR B:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR C:  MELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGP IKGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHL SGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDE DWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPE LVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVV VAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDV VGITRAVCKIVHENADVEEALKEIR D:  MELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGP IKGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHL SGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDE DWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPE LVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVV VAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDV VGITRAVCKIVHENADVEEALKEIRK E:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR F:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR G:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR H:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR I:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR J:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR K:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR L:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIRK M:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR N:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR O:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR P:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR Q:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR R:  MELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGP IKGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHL SGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDE DWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPE LVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVV VAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDV VGITRAVCKIVHENADVEEALKEIRK S:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR T:  ELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPI KGLIDIRKTVNDVAEGGANAVLLHKGIVRHGDVGLIIHLS GGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDED WEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPEL VAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVV AGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVV GITRAVCKIVHENADVEEALKEIR 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 6) chain A residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P A 501 source : AC1 7) chain A residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 16) chain B residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P B 501 source : AC2 17) chain B residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 26) chain C residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P C 501 source : AC3 27) chain C residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 36) chain D residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P D 501 source : AC4 37) chain D residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 46) chain E residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P E 501 source : AC5 47) chain E residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 56) chain F residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P F 501 source : AC6 57) chain F residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 66) chain G residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P G 501 source : AC7 67) chain G residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 76) chain H residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P H 501 source : AC8 77) chain H residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 86) chain I residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P I 501 source : AC9 87) chain I residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 96) chain J residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P J 501 source : BC1 97) chain J residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 106) chain K residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P K 501 source : BC2 107) chain K residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 116) chain L residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P L 501 source : BC3 117) chain L residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 126) chain M residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P M 501 source : BC4 127) chain M residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 136) chain N residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P N 501 source : BC5 137) chain N residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 146) chain O residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P O 501 source : BC6 147) chain O residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 156) chain P residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P P 501 source : BC7 157) chain P residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 166) chain Q residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P Q 501 source : BC8 167) chain Q residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 176) chain R residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P R 501 source : BC9 177) chain R residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 186) chain S residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P S 501 source : CC1 187) chain S residue 210 type sequence G 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 208 type sequence A description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 196) chain T residue 209 type sequence G description BINDING SITE FOR RESIDUE 13P T 501 source : CC2 197) chain T residue 210 type sequence G 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 B residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 202) chain C residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 203) chain D residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 204) chain E residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 205) chain F residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 206) chain G residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 207) chain H residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 208) chain I residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 209) chain J residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 210) chain K residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 211) chain L residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 212) chain M residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 213) chain N residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 214) chain O residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 215) chain P residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 216) chain Q residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 217) chain R residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 218) chain S residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 219) chain T residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 220) chain A residue 33 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI1 221) chain B residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 222) chain C residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 223) chain D residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 224) chain E residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 225) chain F residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 226) chain G residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 227) chain H residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 228) chain I residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 229) chain J residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 230) chain K residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 231) chain L residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 232) chain M residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 233) chain N residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 234) chain O residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 235) chain P residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 236) chain Q residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 237) chain R residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 238) chain S residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 239) chain T residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 240) chain A residue 153 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI2 241) 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 242) 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 243) 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 244) 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 245) 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 246) 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 247) 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 248) 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 249) 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 250) 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 251) 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 252) 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 253) 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 254) 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 255) 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 256) 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 257) 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 258) 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 259) 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 260) 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 261) chain A residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 262) chain C residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 263) chain C residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 264) chain C residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 265) chain D residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 266) chain D residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 267) chain D residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 268) chain D residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 269) chain E residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 270) chain E residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 271) chain E residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 272) chain A residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 273) chain E residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 274) chain F residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 275) chain F residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 276) chain F residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 277) chain F residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 278) chain G residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 279) chain G residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 280) chain G residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 281) chain G residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 282) chain H residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 283) chain A residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 284) chain H residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 285) chain H residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 286) chain H residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 287) chain I residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 288) chain I residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 289) chain I residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 290) chain I residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 291) chain J residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 292) chain J residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 293) chain J residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 294) chain A residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 295) chain J residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 296) chain K residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 297) chain K residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 298) chain K residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 299) chain K residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 300) chain L residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 301) chain L residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 302) chain L residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 303) chain L residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 304) chain M residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 305) chain B residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 306) chain M residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 307) chain M residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 308) chain M residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 309) chain N residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 310) chain N residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 311) chain N residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 312) chain N residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 313) chain O residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 314) chain O residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 315) chain O residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 316) chain B residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 317) chain O residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 318) chain P residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 319) chain P residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 320) chain P residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 321) chain P residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 322) chain Q residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 323) chain Q residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 324) chain Q residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 325) chain Q residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 326) chain R residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 327) chain B residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 328) chain R residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 329) chain R residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 330) chain R residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 331) chain S residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 332) chain S residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 333) chain S residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 334) chain S residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 335) chain T residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 336) chain T residue 153 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 337) chain T residue 209 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 338) chain B residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 339) chain T residue 237 type BINDING sequence G description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4 340) chain C residue 33 type BINDING sequence D description BINDING => ECO:0000305|PubMed:17713928 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links