eF-site ID 1acm-ABCD PDB Code 1acm Chain A, B, C, D click to enlarge Title ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY Classification TRANSFERASE (CARBAMOYL-P,ASPARTATE) Compound ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN Source null (PYRI_ECOLI) Sequence A:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTATRLSFQTSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL B:  GVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLN LPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQATVNRID NYEVVGKSRPSLPERIDNVLVCPNSNCISHAEPVSSSFAV RKRANDIALKCKYCEKEFSHNVVLAN C:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTATRLSFQTSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL D:  GVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLN LPSGEMGRKDLIKIENTFLSEDQVDQLALYAPQATVNRID NYEVVGKSRPSLPERIDNVLVCPNSNCISHAEPVSSSFAV RKRANDIALKCKYCEKEFSHNVVLAN Description Functional site 1) chain A residue 52 type sequence S description PAL BINDING SITES OF CHAINS A source : PAA 2) chain A residue 54 type sequence A description PAL BINDING SITES OF CHAINS A source : PAA 3) chain A residue 55 type sequence T description PAL BINDING SITES OF CHAINS A source : PAA 4) chain A residue 80 type sequence S description PAL BINDING SITES OF CHAINS A source : PAA 5) chain A residue 84 type sequence K description PAL BINDING SITES OF CHAINS A source : PAA 6) chain A residue 134 type sequence H description PAL BINDING SITES OF CHAINS A source : PAA 7) chain A residue 167 type sequence R description PAL BINDING SITES OF CHAINS A source : PAA 8) chain A residue 229 type sequence R description PAL BINDING SITES OF CHAINS A source : PAA 9) chain A residue 231 type sequence Q description PAL BINDING SITES OF CHAINS A source : PAA 10) chain B residue 109 type sequence C description ZN BINDING SITES OF CHAINS B source : ZNB 11) chain B residue 114 type sequence C description ZN BINDING SITES OF CHAINS B source : ZNB 12) chain B residue 138 type sequence C description ZN BINDING SITES OF CHAINS B source : ZNB 13) chain B residue 141 type sequence C description ZN BINDING SITES OF CHAINS B source : ZNB 14) chain C residue 52 type sequence S description PAL BINDING SITES OF CHAINS C source : PAC 15) chain C residue 54 type sequence A description PAL BINDING SITES OF CHAINS C source : PAC 16) chain C residue 55 type sequence T description PAL BINDING SITES OF CHAINS C source : PAC 17) chain C residue 80 type sequence S description PAL BINDING SITES OF CHAINS C source : PAC 18) chain C residue 84 type sequence K description PAL BINDING SITES OF CHAINS C source : PAC 19) chain C residue 134 type sequence H description PAL BINDING SITES OF CHAINS C source : PAC 20) chain C residue 167 type sequence R description PAL BINDING SITES OF CHAINS C source : PAC 21) chain C residue 229 type sequence R description PAL BINDING SITES OF CHAINS C source : PAC 22) chain C residue 231 type sequence Q description PAL BINDING SITES OF CHAINS C source : PAC 23) chain D residue 109 type sequence C description ZN BINDING SITES OF CHAINS D source : ZND 24) chain D residue 114 type sequence C description ZN BINDING SITES OF CHAINS D source : ZND 25) chain D residue 138 type sequence C description ZN BINDING SITES OF CHAINS D source : ZND 26) chain D residue 141 type sequence C description ZN BINDING SITES OF CHAINS D source : ZND 27) chain B residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 28) chain B residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 29) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 30) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 31) chain D residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 32) chain D residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 33) chain D residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 34) chain D residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 35) chain A residue 52 type sequence S description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 36) chain A residue 53 type sequence T description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 37) chain A residue 54 type sequence A description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 38) chain A residue 55 type sequence T description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 39) chain A residue 80 type sequence S description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 40) chain A residue 84 type sequence K description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 41) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 42) chain A residue 134 type sequence H description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 43) chain A residue 137 type sequence Q description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 44) chain A residue 167 type sequence R description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 45) chain A residue 229 type sequence R description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 46) chain A residue 231 type sequence Q description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 47) chain A residue 267 type sequence L description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 48) chain A residue 268 type sequence P description BINDING SITE FOR RESIDUE PAL A 311 source : AC3 49) chain C residue 52 type sequence S description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 50) chain C residue 53 type sequence T description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 51) chain C residue 54 type sequence A description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 52) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 53) chain C residue 80 type sequence S description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 54) chain C residue 84 type sequence K description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 55) chain C residue 105 type sequence R description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 56) chain C residue 134 type sequence H description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 57) chain C residue 167 type sequence R description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 58) chain C residue 229 type sequence R description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 59) chain C residue 231 type sequence Q description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 60) chain C residue 267 type sequence L description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 61) chain C residue 268 type sequence P description BINDING SITE FOR RESIDUE PAL C 311 source : AC4 62) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 63) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 64) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 65) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 66) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 67) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 68) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 69) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 70) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 71) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 72) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 73) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 74) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 75) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 76) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 77) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 78) chain B residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 79) chain B residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 80) chain B residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 81) chain B residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 82) chain D residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 83) chain D residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 84) chain D residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 85) chain D residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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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