eF-site ID 6at1-ABCD PDB Code 6at1 Chain A, B, C, D click to enlarge Title STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION 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 B residue 109 type sequence C description zinc binding site source : ZNB 2) chain B residue 114 type sequence C description zinc binding site source : ZNB 3) chain B residue 138 type sequence C description zinc binding site source : ZNB 4) chain B residue 141 type sequence C description zinc binding site source : ZNB 5) chain D residue 109 type sequence C description zinc binding site source : ZND 6) chain D residue 114 type sequence C description zinc binding site source : ZND 7) chain D residue 138 type sequence C description zinc binding site source : ZND 8) chain D residue 141 type sequence C description zinc binding site source : ZND 9) chain B residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 10) chain B residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 11) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 12) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 13) chain D residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 14) chain D residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 15) chain D residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 16) chain D residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 17) 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 18) 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 19) 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 20) 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 21) 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 22) 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 23) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 24) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 25) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 26) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 27) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 28) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 29) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 30) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 31) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 32) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 33) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 34) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 35) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 36) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 37) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 38) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 39) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 40) chain D residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 41) chain D residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 42) chain D residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 43) chain B residue 109 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 44) chain B residue 114 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 45) chain B residue 138 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 46) chain B residue 141 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 47) chain D residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1

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