eF-site ID 4at1-ABCD PDB Code 4at1 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 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 B residue 109 type sequence C description zn binding site source : ZNB 2) chain B residue 114 type sequence C description zn binding site source : ZNB 3) chain B residue 138 type sequence C description zn binding site source : ZNB 4) chain B residue 141 type sequence C description zn binding site source : ZNB 5) chain B residue 9 type sequence V description atp binding site source : ATB 6) chain B residue 10 type sequence E description atp binding site source : ATB 7) chain B residue 11 type sequence A description atp binding site source : ATB 8) chain B residue 12 type sequence I description atp binding site source : ATB 9) chain B residue 19 type sequence D description atp binding site source : ATB 10) chain B residue 58 type sequence L description atp binding site source : ATB 11) chain B residue 60 type sequence K description atp binding site source : ATB 12) chain B residue 84 type sequence N description atp binding site source : ATB 13) chain B residue 89 type sequence Y description atp binding site source : ATB 14) chain B residue 91 type sequence V description atp binding site source : ATB 15) chain B residue 94 type sequence K description atp binding site source : ATB 16) chain D residue 109 type sequence C description zn binding site source : ZND 17) chain D residue 114 type sequence C description zn binding site source : ZND 18) chain D residue 138 type sequence C description zn binding site source : ZND 19) chain D residue 141 type sequence C description zn binding site source : ZND 20) chain D residue 9 type sequence V description atp binding site source : ATD 21) chain D residue 10 type sequence E description atp binding site source : ATD 22) chain D residue 11 type sequence A description atp binding site source : ATD 23) chain D residue 12 type sequence I description atp binding site source : ATD 24) chain D residue 19 type sequence D description atp binding site source : ATD 25) chain D residue 58 type sequence L description atp binding site source : ATD 26) chain D residue 60 type sequence K description atp binding site source : ATD 27) chain D residue 84 type sequence N description atp binding site source : ATD 28) chain D residue 89 type sequence Y description atp binding site source : ATD 29) chain D residue 91 type sequence V description atp binding site source : ATD 30) chain D residue 94 type sequence K description atp binding site source : ATD 31) chain B residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 32) chain B residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 33) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 34) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 35) chain D residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 36) chain D residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 37) chain D residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 38) chain D residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 39) chain B residue 9 type sequence V description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 40) chain B residue 10 type sequence E description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 41) chain B residue 11 type sequence A description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 42) chain B residue 12 type sequence I description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 43) chain B residue 17 type sequence V description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 44) chain B residue 19 type sequence D description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 45) chain B residue 58 type sequence L description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 46) chain B residue 60 type sequence K description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 47) chain B residue 84 type sequence N description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 48) chain B residue 89 type sequence Y description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 49) chain B residue 91 type sequence V description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 50) chain B residue 94 type sequence K description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 51) chain B residue 130 type sequence R description BINDING SITE FOR RESIDUE ATP B 155 source : AC3 52) chain D residue 9 type sequence V description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 53) chain D residue 10 type sequence E description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 54) chain D residue 11 type sequence A description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 55) chain D residue 12 type sequence I description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 56) chain D residue 17 type sequence V description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 57) chain D residue 58 type sequence L description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 58) chain D residue 60 type sequence K description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 59) chain D residue 86 type sequence I description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 60) chain D residue 89 type sequence Y description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 61) chain D residue 90 type sequence E description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 62) chain D residue 94 type sequence K description BINDING SITE FOR RESIDUE ATP D 155 source : AC4 63) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 64) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 65) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 66) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 67) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 68) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 69) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 70) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 71) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 72) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 73) chain B residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 74) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 75) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 76) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 77) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 78) chain C residue 269 type BINDING sequence R 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 C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 87) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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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