eF-site ID 3at1-ABCD PDB Code 3at1 Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH Classification TRANSFERASE (CARBAMOYL-P,ASPARTATE) Compound ASPARTATE CARBAMOYLTRANSFERASE (T STATE), CATALYTIC CHAIN Source null (PYRI_ECOLI) Sequence A:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL B:  GVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLN LPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQATVNRID NYEVVGKSRPSLPERIDNVLVCPNSNCISHAEPVSSSFAV RKRANDIALKCKYCEKEFSHNVVLAN C:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL D:  GVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLN LPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQATVNRID NYEVVGKSRPSLPERIDNVLVCPNSNCISHAEPVSSSFAV RKRANDIALKCKYCEKEFSHNVVLAN Description Functional site 1) chain A residue 54 type sequence R description PCT binding site source : PAA 2) chain A residue 55 type sequence T description PCT binding site source : PAA 3) chain A residue 105 type sequence R description PCT binding site source : PAA 4) chain A residue 134 type sequence H description PCT binding site source : PAA 5) chain A residue 137 type sequence Q description PCT binding site source : PAA 6) chain A residue 266 type sequence P description PCT binding site source : PAA 7) chain A residue 267 type sequence L description PCT binding site source : PAA 8) chain C residue 54 type sequence R description PCT binding site source : PAC 9) chain C residue 55 type sequence T description PCT binding site source : PAC 10) chain C residue 105 type sequence R description PCT binding site source : PAC 11) chain C residue 134 type sequence H description PCT binding site source : PAC 12) chain C residue 137 type sequence Q description PCT binding site source : PAC 13) chain C residue 266 type sequence P description PCT binding site source : PAC 14) chain C residue 267 type sequence L description PCT binding site source : PAC 15) chain B residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 16) chain B residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 17) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 18) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 19) chain D residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 20) chain D residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 21) chain D residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 22) chain D residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 23) chain A residue 52 type sequence S description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 24) chain A residue 53 type sequence T description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 25) chain A residue 54 type sequence R description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 26) chain A residue 55 type sequence T description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 27) chain A residue 81 type sequence L description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 28) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 29) chain A residue 134 type sequence H description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 30) chain A residue 137 type sequence Q description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 31) chain A residue 266 type sequence P description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 32) chain A residue 267 type sequence L description BINDING SITE FOR RESIDUE PCT A 311 source : AC3 33) chain C residue 52 type sequence S description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 34) chain C residue 54 type sequence R description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 35) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 36) chain C residue 105 type sequence R description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 37) chain C residue 137 type sequence Q description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 38) chain A residue 85 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 168 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 230 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 41) chain C residue 85 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 42) chain C residue 168 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 43) chain C residue 230 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 45) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 46) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 47) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 48) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 49) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 50) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 51) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 52) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 53) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 54) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 55) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 56) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 57) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 58) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 59) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 60) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 61) chain D residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 62) chain D residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 63) chain D residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 64) chain D residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 65) chain B residue 109 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 66) chain B residue 114 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 67) chain B residue 138 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 68) chain B residue 141 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1

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