eF-site ID 1d09-ABCD PDB Code 1d09 Chain A, B, C, D click to enlarge Title ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA) Classification TRANSFERASE Compound ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN Source Escherichia coli (strain K12) (PYRI_ECOLI) Sequence A:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTQGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL B:  MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQ RITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQ ATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEP VSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN C:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTQGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL D:  MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQ RITIGLNLPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQ ATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEP VSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN Description Functional site 1) chain B residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN B 1313 source : AC1 2) chain B residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN B 1313 source : AC1 3) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN B 1313 source : AC1 4) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN B 1313 source : AC1 5) chain D residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN D 1314 source : AC2 6) chain D residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN D 1314 source : AC2 7) chain D residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN D 1314 source : AC2 8) chain D residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN D 1314 source : AC2 9) chain A residue 52 type sequence S description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 10) chain A residue 53 type sequence T description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 11) chain A residue 54 type sequence R description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 12) chain A residue 55 type sequence T description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 13) chain A residue 80 type sequence S description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 14) chain A residue 84 type sequence K description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 15) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 16) chain A residue 134 type sequence H description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 17) chain A residue 137 type sequence Q description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 18) chain A residue 167 type sequence R description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 19) chain A residue 229 type sequence R description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 20) chain A residue 231 type sequence Q description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 21) chain A residue 267 type sequence L description BINDING SITE FOR RESIDUE PAL A 1311 source : AC3 22) chain C residue 52 type sequence S description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 23) chain C residue 53 type sequence T description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 24) chain C residue 54 type sequence R description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 25) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 26) chain C residue 80 type sequence S description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 27) chain C residue 84 type sequence K description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 28) chain C residue 105 type sequence R description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 29) chain C residue 134 type sequence H description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 30) chain C residue 167 type sequence R description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 31) chain C residue 168 type sequence T description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 32) chain C residue 229 type sequence R description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 33) chain C residue 267 type sequence L description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 34) chain C residue 268 type sequence P description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 35) chain A residue 54 type catalytic sequence R description 405 source MCSA : MCSA1 36) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 37) chain A residue 84 type catalytic sequence K description 405 source MCSA : MCSA1 38) chain A residue 105 type catalytic sequence R description 405 source MCSA : MCSA1 39) chain A residue 134 type catalytic sequence H description 405 source MCSA : MCSA1 40) chain C residue 54 type catalytic sequence R description 405 source MCSA : MCSA2 41) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 42) chain C residue 84 type catalytic sequence K description 405 source MCSA : MCSA2 43) chain C residue 105 type catalytic sequence R description 405 source MCSA : MCSA2 44) chain C residue 134 type catalytic sequence H description 405 source MCSA : MCSA2 45) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 46) chain B residue 109 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 47) chain C residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 48) chain C residue 134 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 49) chain C residue 137 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI1 50) chain C residue 267 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI1 51) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 52) chain B residue 114 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 53) chain B residue 138 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 54) chain B residue 141 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 55) chain D residue 109 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 56) chain D residue 114 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 57) chain D residue 138 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 58) chain D residue 141 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 59) chain C residue 55 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 60) chain A residue 84 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 167 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 62) chain A residue 229 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 63) chain C residue 84 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 64) chain C residue 167 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 65) chain C residue 229 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2

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