eF-site ID 1zud-1234 PDB Code 1zud Chain 1, 2, 3, 4 click to enlarge Title Structure of ThiS-ThiF protein complex Classification TRANSFERASE/BIOSYNTHETIC PROTEIN Compound Adenylyltransferase thiF Source Escherichia coli (strain K12) (THIS_ECOLI) Sequence 1:  MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLG TPAALYLAGAGVGTLVLADDDDVHLSNLQRQILFTTEDID RPKSQVSQQRLTQLNPDIQLTALQQRLTGEALKDAVARAD VVLDCTDNMATRQEINAACVALNTPLITASAVGFGGQLMV LTPPWEQGCYRCLWPAGVVGPVVGVMGTLQALEAIKLLSG IETPAGELRLFDGKSSQWRSLALRRASGCPVCGG 2:  QILFNDQAMQCAAGQTVHELLEQLDQRQAGAALAINQQIV PREQWAQHIVQDGDQILLFQVIAGG 3:  MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLG TPAALYLAGAGVGTLVLADDDDVHLSNLQRQILFTTEDID RPKSQVSQQRLTQLNPDIQLTALQQRLTGEALKDAVARAD VVLDCTDNMATRQEINAACVALNTPLITASAVGFGGQLMV LTPPWEQGCYRCLWPDNQEPTAGVVGPVVGVMGTLQALEA IKLLSGIETPAGELRLFDGKSSQWRSLALRRASGCPVCGG 4:  MQILFNDQAMQCAAGQTVHELLEQLDQRQAGAALAINQQI VPREQWAQHIVQDGDQILLFQVIAGG Description Functional site 1) chain 1 residue 169 type sequence C description BINDING SITE FOR RESIDUE ZN 1 501 source : AC1 2) chain 1 residue 172 type sequence C description BINDING SITE FOR RESIDUE ZN 1 501 source : AC1 3) chain 1 residue 240 type sequence C description BINDING SITE FOR RESIDUE ZN 1 501 source : AC1 4) chain 1 residue 243 type sequence C description BINDING SITE FOR RESIDUE ZN 1 501 source : AC1 5) chain 3 residue 169 type sequence C description BINDING SITE FOR RESIDUE ZN 3 502 source : AC2 6) chain 3 residue 172 type sequence C description BINDING SITE FOR RESIDUE ZN 3 502 source : AC2 7) chain 3 residue 240 type sequence C description BINDING SITE FOR RESIDUE ZN 3 502 source : AC2 8) chain 3 residue 243 type sequence C description BINDING SITE FOR RESIDUE ZN 3 502 source : AC2 9) chain 1 residue 14 type sequence L description BINDING SITE FOR RESIDUE CA 3 601 source : AC3 10) chain 1 residue 16 type sequence D description BINDING SITE FOR RESIDUE CA 3 601 source : AC3 11) chain 3 residue 14 type sequence L description BINDING SITE FOR RESIDUE CA 3 601 source : AC3 12) chain 3 residue 16 type sequence D description BINDING SITE FOR RESIDUE CA 3 601 source : AC3 13) chain 1 residue 243 type sequence C description BINDING SITE FOR RESIDUE CA 1 602 source : AC4 14) chain 1 residue 116 type sequence V description BINDING SITE FOR RESIDUE NA 1 701 source : AC5 15) chain 1 residue 117 type sequence A description BINDING SITE FOR RESIDUE NA 1 701 source : AC5 16) chain 1 residue 119 type sequence A description BINDING SITE FOR RESIDUE NA 1 701 source : AC5 17) chain 1 residue 144 type sequence T description BINDING SITE FOR RESIDUE NA 1 701 source : AC5 18) chain 3 residue 116 type sequence V description BINDING SITE FOR RESIDUE NA 3 702 source : AC6 19) chain 3 residue 117 type sequence A description BINDING SITE FOR RESIDUE NA 3 702 source : AC6 20) chain 3 residue 119 type sequence A description BINDING SITE FOR RESIDUE NA 3 702 source : AC6 21) chain 3 residue 144 type sequence T description BINDING SITE FOR RESIDUE NA 3 702 source : AC6 22) chain 1 residue 169 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 23) chain 1 residue 172 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 24) chain 1 residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 25) chain 1 residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 26) chain 3 residue 169 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 27) chain 3 residue 172 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 28) chain 3 residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 29) chain 3 residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16388576 source Swiss-Prot : SWS_FT_FI3 30) chain 2 residue 66 type MOD_RES sequence G description Glycyl adenylate; alternate => ECO:0000269|PubMed:9632726 source Swiss-Prot : SWS_FT_FI1 31) chain 4 residue 66 type MOD_RES sequence G description Glycyl adenylate; alternate => ECO:0000269|PubMed:9632726 source Swiss-Prot : SWS_FT_FI1 32) chain 2 residue 66 type CROSSLNK sequence G description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 33) chain 3 residue 59 type CROSSLNK sequence D description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 34) chain 3 residue 70 type CROSSLNK sequence R description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 35) chain 3 residue 83 type CROSSLNK sequence K description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 36) chain 3 residue 107 type CROSSLNK sequence L description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 37) chain 3 residue 127 type CROSSLNK sequence D description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 38) chain 1 residue 38 type CROSSLNK sequence G description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 39) chain 4 residue 66 type CROSSLNK sequence G description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 40) chain 1 residue 70 type CROSSLNK sequence R description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 41) chain 1 residue 83 type CROSSLNK sequence K description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 42) chain 1 residue 107 type CROSSLNK sequence L description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 43) chain 1 residue 127 type CROSSLNK sequence D description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 44) chain 3 residue 11 type CROSSLNK sequence R description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2 45) chain 3 residue 38 type CROSSLNK sequence G description Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate source Swiss-Prot : SWS_FT_FI2

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