eF-site ID 1at1-ABCD PDB Code 1at1 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 P*H Classification TRANSFERASE (CARBAMOYL-P,ASPARTATE) Compound ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN Source Escherichia coli (strain K12) (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 BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 2) chain A residue 55 type sequence T description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 3) chain A residue 105 type sequence R description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 4) chain A residue 134 type sequence H description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 5) chain A residue 137 type sequence Q description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 6) chain A residue 167 type sequence R description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 7) chain A residue 229 type sequence R description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 8) chain A residue 231 type sequence Q description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 9) chain A residue 266 type sequence P description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 10) chain A residue 267 type sequence L description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS A source : PMA 11) chain B residue 109 type sequence C description ZN BINDING SITES OF CHAINS B source : ZNB 12) chain B residue 114 type sequence C description ZN BINDING SITES OF CHAINS B source : ZNB 13) chain B residue 138 type sequence C description ZN BINDING SITES OF CHAINS B source : ZNB 14) chain B residue 141 type sequence C description ZN BINDING SITES OF CHAINS B source : ZNB 15) chain C residue 54 type sequence R description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 16) chain C residue 55 type sequence T description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 17) chain C residue 105 type sequence R description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 18) chain C residue 134 type sequence H description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 19) chain C residue 137 type sequence Q description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 20) chain C residue 167 type sequence R description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 21) chain C residue 229 type sequence R description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 22) chain C residue 231 type sequence Q description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 23) chain C residue 266 type sequence P description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 24) chain C residue 267 type sequence L description BINDING SITES OF COMBINED MALONATE (MLI) AND PHOSPHONOACETAMIDE (PCT) MOLECULES OF CHAINS C source : PMC 25) chain D residue 109 type sequence C description ZN BINDING SITES OF CHAINS D source : ZND 26) chain D residue 114 type sequence C description ZN BINDING SITES OF CHAINS D source : ZND 27) chain D residue 138 type sequence C description ZN BINDING SITES OF CHAINS D source : ZND 28) chain D residue 141 type sequence C description ZN BINDING SITES OF CHAINS D source : ZND 29) chain A residue 84 type sequence K description BINDING SITE FOR RESIDUE MLI A 312 source : AC1 30) chain A residue 134 type sequence H description BINDING SITE FOR RESIDUE MLI A 312 source : AC1 31) chain A residue 167 type sequence R description BINDING SITE FOR RESIDUE MLI A 312 source : AC1 32) chain A residue 168 type sequence T description BINDING SITE FOR RESIDUE MLI A 312 source : AC1 33) chain A residue 229 type sequence R description BINDING SITE FOR RESIDUE MLI A 312 source : AC1 34) chain A residue 231 type sequence Q description BINDING SITE FOR RESIDUE MLI A 312 source : AC1 35) chain C residue 84 type sequence K description BINDING SITE FOR RESIDUE MLI C 312 source : AC2 36) chain C residue 105 type sequence R description BINDING SITE FOR RESIDUE MLI C 312 source : AC2 37) chain C residue 134 type sequence H description BINDING SITE FOR RESIDUE MLI C 312 source : AC2 38) chain C residue 167 type sequence R description BINDING SITE FOR RESIDUE MLI C 312 source : AC2 39) chain C residue 168 type sequence T description BINDING SITE FOR RESIDUE MLI C 312 source : AC2 40) chain C residue 229 type sequence R description BINDING SITE FOR RESIDUE MLI C 312 source : AC2 41) chain C residue 231 type sequence Q description BINDING SITE FOR RESIDUE MLI C 312 source : AC2 42) chain C residue 268 type sequence P description BINDING SITE FOR RESIDUE MLI C 312 source : AC2 43) chain B residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC3 44) chain B residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC3 45) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC3 46) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC3 47) chain D residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC4 48) chain D residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC4 49) chain D residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC4 50) chain D residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC4 51) chain A residue 52 type sequence S description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 52) chain A residue 53 type sequence T description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 53) chain A residue 54 type sequence R description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 54) chain A residue 55 type sequence T description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 55) chain A residue 80 type sequence S description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 56) chain A residue 84 type sequence K description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 57) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 58) chain A residue 134 type sequence H description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 59) chain A residue 137 type sequence Q description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 60) chain A residue 266 type sequence P description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 61) chain A residue 267 type sequence L description BINDING SITE FOR RESIDUE PCT A 311 source : AC5 62) chain C residue 51 type sequence A description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 63) chain C residue 52 type sequence S description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 64) chain C residue 53 type sequence T description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 65) chain C residue 54 type sequence R description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 66) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 67) chain C residue 80 type sequence S description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 68) chain C residue 84 type sequence K description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 69) chain C residue 105 type sequence R description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 70) chain C residue 134 type sequence H description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 71) chain C residue 137 type sequence Q description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 72) chain C residue 267 type sequence L description BINDING SITE FOR RESIDUE PCT C 311 source : AC6 73) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 74) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 75) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 76) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 77) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 78) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 79) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 80) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 81) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 82) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 83) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 84) chain B residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 85) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 86) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 87) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 88) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 89) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 90) chain B residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 91) chain B residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 92) chain B residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 93) chain D residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 94) chain D residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 95) chain D residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 96) chain D residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 97) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 98) 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 99) 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 100) 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 101) 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 102) 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 103) 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

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