eF-site ID 1zfn-ABCD PDB Code 1zfn Chain A, B, C, D click to enlarge Title Structural Analysis of Escherichia coli ThiF Classification TRANSFERASE Compound Adenylyltransferase thiF Source Escherichia coli (strain K12) (THIF_ECOLI) Sequence A:  MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLG TPAALYLAGAGVGTLVLADDDDVHLSNLQRQILFTTEDID RPKSQVSQQRLTQLNPDIQLTALQQRLTGEALKDAVARAD VVLDCTDNMATRQEINAACVALNTPLITASAVGFGGQLMV LTPPWEQGCYRCLWPDNQEPERNCRTAGVVGPVVGVMGTL QALEAIKLLSGIETPAGELRLFDGKSSQWRSLALRRASGC PVCG B:  MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLG TPAALYLAGAGVGTLVLADDDDVHLSNLQRQILFTTEDID RPKSQVSQQRLTQLNPDIQLTALQQRLTGEALKDAVARAD VVLDCTDNMATRQEINAACVALNTPLITASAVGFGGQLMV LTPPWEQGCYRCLWAGVVGPVVGVMGTLQALEAIKLLSGI ETPAGELRLFDGKSSQWRSLALRRASGCPVCG C:  MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLG TPAALYLAGAGVGTLVLADDDDVHLSNLQRQILFTTEDID RPKSQVSQQRLTQLNPDIQLTALQQRLTGEALKDAVARAD VVLDCTDNMATRQEINAACVALNTPLITASAVGFGGQLMV LTPPWEQGCYRCLWPDNQEPERNCRTAGVVGPVVGVMGTL QALEAIKLLSGIETPAGELRLFDGKSSQWRSLALRRASGC PVCG D:  MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLG TPAALYLAGAGVGTLVLADDDDVHLSNLQRQILFTTEDID RPKSQVSQQRLTQLNPDIQLTALQQRLTGEALKDAVARAD VVLDCTDNMATRQEINAACVALNTPLITASAVGFGGQLMV LTPPWEQGCYRCLWPDNAGVVGPVVGVMGTLQALEAIKLL SGIETPAGELRLFDGKSSQWRSLALRRASGCPVCG Description Functional site 1) chain A residue 169 type sequence C description BINDING SITE FOR RESIDUE ZN A 252 source : AC1 2) chain A residue 172 type sequence C description BINDING SITE FOR RESIDUE ZN A 252 source : AC1 3) chain A residue 240 type sequence C description BINDING SITE FOR RESIDUE ZN A 252 source : AC1 4) chain A residue 243 type sequence C description BINDING SITE FOR RESIDUE ZN A 252 source : AC1 5) chain B residue 169 type sequence C description BINDING SITE FOR RESIDUE ZN B 252 source : AC2 6) chain B residue 172 type sequence C description BINDING SITE FOR RESIDUE ZN B 252 source : AC2 7) chain B residue 240 type sequence C description BINDING SITE FOR RESIDUE ZN B 252 source : AC2 8) chain B residue 242 type sequence V description BINDING SITE FOR RESIDUE ZN B 252 source : AC2 9) chain B residue 243 type sequence C description BINDING SITE FOR RESIDUE ZN B 252 source : AC2 10) chain C residue 169 type sequence C description BINDING SITE FOR RESIDUE ZN C 345 source : AC3 11) chain C residue 172 type sequence C description BINDING SITE FOR RESIDUE ZN C 345 source : AC3 12) chain C residue 240 type sequence C description BINDING SITE FOR RESIDUE ZN C 345 source : AC3 13) chain C residue 243 type sequence C description BINDING SITE FOR RESIDUE ZN C 345 source : AC3 14) chain D residue 169 type sequence C description BINDING SITE FOR RESIDUE ZN D 445 source : AC4 15) chain D residue 172 type sequence C description BINDING SITE FOR RESIDUE ZN D 445 source : AC4 16) chain D residue 240 type sequence C description BINDING SITE FOR RESIDUE ZN D 445 source : AC4 17) chain D residue 243 type sequence C description BINDING SITE FOR RESIDUE ZN D 445 source : AC4 18) chain C residue 34 type sequence I description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 19) chain C residue 35 type sequence G description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 20) chain C residue 37 type sequence G description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 21) chain C residue 38 type sequence G description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 22) chain C residue 59 type sequence D description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 23) chain C residue 61 type sequence D description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 24) chain C residue 66 type sequence S description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 25) chain C residue 67 type sequence N description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 26) chain C residue 70 type sequence R description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 27) chain C residue 71 type sequence Q description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 28) chain C residue 83 type sequence K description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 29) chain C residue 106 type sequence R description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 30) chain C residue 107 type sequence L description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 31) chain C residue 125 type sequence C description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 32) chain C residue 126 type sequence T description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 33) chain C residue 127 type sequence D description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 34) chain C residue 131 type sequence T description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 35) chain D residue 11 type sequence R description BINDING SITE FOR RESIDUE ATP C 346 source : AC5 36) chain C residue 11 type sequence R description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 37) chain D residue 34 type sequence I description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 38) chain D residue 35 type sequence G description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 39) chain D residue 37 type sequence G description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 40) chain D residue 38 type sequence G description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 41) chain D residue 58 type sequence A description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 42) chain D residue 59 type sequence D description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 43) chain D residue 61 type sequence D description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 44) chain D residue 66 type sequence S description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 45) chain D residue 67 type sequence N description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 46) chain D residue 70 type sequence R description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 47) chain D residue 71 type sequence Q description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 48) chain D residue 83 type sequence K description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 49) chain D residue 106 type sequence R description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 50) chain D residue 107 type sequence L description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 51) chain D residue 125 type sequence C description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 52) chain D residue 126 type sequence T description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 53) chain D residue 127 type sequence D description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 54) chain D residue 131 type sequence T description BINDING SITE FOR RESIDUE ATP D 446 source : AC6 55) chain A residue 34 type sequence I description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 56) chain A residue 35 type sequence G description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 57) chain A residue 37 type sequence G description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 58) chain A residue 38 type sequence G description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 59) chain A residue 59 type sequence D description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 60) chain A residue 61 type sequence D description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 61) chain A residue 70 type sequence R description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 62) chain A residue 71 type sequence Q description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 63) chain A residue 83 type sequence K description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 64) chain A residue 105 type sequence Q description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 65) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 66) chain A residue 107 type sequence L description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 67) chain A residue 125 type sequence C description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 68) chain A residue 126 type sequence T description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 69) chain A residue 127 type sequence D description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 70) chain A residue 131 type sequence T description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 71) chain B residue 11 type sequence R description BINDING SITE FOR RESIDUE ATP A 253 source : AC7 72) chain A residue 11 type sequence R description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 73) chain B residue 35 type sequence G description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 74) chain B residue 37 type sequence G description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 75) chain B residue 38 type sequence G description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 76) chain B residue 59 type sequence D description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 77) chain B residue 61 type sequence D description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 78) chain B residue 66 type sequence S description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 79) chain B residue 67 type sequence N description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 80) chain B residue 70 type sequence R description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 81) chain B residue 71 type sequence Q description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 82) chain B residue 83 type sequence K description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 83) chain B residue 105 type sequence Q description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 84) chain B residue 106 type sequence R description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 85) chain B residue 107 type sequence L description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 86) chain B residue 125 type sequence C description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 87) chain B residue 126 type sequence T description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 88) chain B residue 127 type sequence D description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 89) chain B residue 131 type sequence T description BINDING SITE FOR RESIDUE ATP B 253 source : AC8 90) chain A residue 184 type ACT_SITE sequence C description Glycyl persulfide ester intermediate source Swiss-Prot : SWS_FT_FI1 91) chain C residue 184 type ACT_SITE sequence C description Glycyl persulfide ester intermediate source Swiss-Prot : SWS_FT_FI1 92) chain A residue 11 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 93) chain B residue 59 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 94) chain B residue 70 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 95) chain B residue 83 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 96) chain B residue 107 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 97) chain B residue 127 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 98) chain C residue 11 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 99) chain C residue 38 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 100) chain C residue 59 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 101) chain C residue 70 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 102) chain C residue 83 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 103) chain A residue 38 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 104) chain C residue 107 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 105) chain C residue 127 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 106) chain D residue 11 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 107) chain D residue 38 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 108) chain D residue 59 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 109) chain D residue 70 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 110) chain D residue 83 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 111) chain D residue 107 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 112) chain D residue 127 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 113) chain A residue 59 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 114) chain A residue 70 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 115) chain A residue 83 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 116) chain A residue 107 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 117) chain A residue 127 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 118) chain B residue 11 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 119) chain B residue 38 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 120) chain A residue 169 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 121) chain C residue 172 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 122) chain C residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 123) chain C residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 124) chain D residue 169 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 125) chain D residue 172 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 126) chain D residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 127) chain D residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 128) chain A residue 172 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 129) chain A residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 130) chain A residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 131) chain B residue 169 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 132) chain B residue 172 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 133) chain B residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 134) chain B residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 135) chain C residue 169 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 136) chain A residue 184 type CROSSLNK sequence C description Glycyl cysteine dithioester (Cys-Gly) (interchain with G-Cter in ThiS) source Swiss-Prot : SWS_FT_FI4 137) chain C residue 184 type CROSSLNK sequence C description Glycyl cysteine dithioester (Cys-Gly) (interchain with G-Cter in ThiS) source Swiss-Prot : SWS_FT_FI4

Display surface Download Links