eF-site ID 2air-ABGH PDB Code 2air Chain A, B, G, H click to enlarge Title T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme Classification TRANSFERASE Compound Aspartate carbamoyltransferase catalytic chain Source (PYRI_ECOLI) Sequence A:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL B:  MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQ RITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQ ATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEP VSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN G:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL H:  MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQ RITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQ ATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEP VSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN Description Functional site 1) chain B residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN B 800 source : AC1 2) chain B residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN B 800 source : AC1 3) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN B 800 source : AC1 4) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN B 800 source : AC1 5) chain H residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN H 801 source : AC2 6) chain H residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN H 801 source : AC2 7) chain H residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN H 801 source : AC2 8) chain H residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN H 801 source : AC2 9) chain A residue 54 type sequence R description BINDING SITE FOR RESIDUE CP A 802 source : AC3 10) chain A residue 55 type sequence T description BINDING SITE FOR RESIDUE CP A 802 source : AC3 11) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE CP A 802 source : AC3 12) chain A residue 134 type sequence H description BINDING SITE FOR RESIDUE CP A 802 source : AC3 13) chain G residue 54 type sequence R description BINDING SITE FOR RESIDUE CP G 803 source : AC4 14) chain G residue 55 type sequence T description BINDING SITE FOR RESIDUE CP G 803 source : AC4 15) chain G residue 105 type sequence R description BINDING SITE FOR RESIDUE CP G 803 source : AC4 16) chain G residue 134 type sequence H description BINDING SITE FOR RESIDUE CP G 803 source : AC4 17) chain G residue 229 type sequence R description BINDING SITE FOR RESIDUE CP G 803 source : AC4 18) chain G residue 51 type sequence A description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 19) chain G residue 52 type sequence S description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 20) chain G residue 54 type sequence R description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 21) chain G residue 55 type sequence T description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 22) chain G residue 80 type sequence S description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 23) chain G residue 105 type sequence R description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 24) chain A residue 51 type sequence A description BINDING SITE FOR RESIDUE AL0 A 805 source : AC6 25) chain A residue 52 type sequence S description BINDING SITE FOR RESIDUE AL0 A 805 source : AC6 26) chain A residue 53 type sequence T description BINDING SITE FOR RESIDUE AL0 A 805 source : AC6 27) chain A residue 54 type sequence R description BINDING SITE FOR RESIDUE AL0 A 805 source : AC6 28) chain A residue 80 type sequence S description BINDING SITE FOR RESIDUE AL0 A 805 source : AC6 29) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE AL0 A 805 source : AC6 30) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 31) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 32) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 33) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 34) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 35) chain G residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 36) chain G residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 37) chain G residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 38) chain G residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 39) chain G residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 40) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 41) chain B residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 42) chain G residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 43) chain G residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 44) chain G residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 45) chain G residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 46) chain G residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 47) chain B residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 48) chain B residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 49) chain B residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 50) chain H residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 51) chain H residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 52) chain H residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 53) chain H residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 54) chain G residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 55) 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 56) 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 57) 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 58) chain G residue 85 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 59) chain G residue 168 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 60) chain G 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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