eF-site ID 5at1-ABCD PDB Code 5at1 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 (1)  ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCARBAMYLASE) (T STATE) (E.C.2.1.3.2) COMPLEX WITH CYTIDINE 5-PRIME-TRIPHOSPHATE (CTP) Functional site 1) chain B residue 12 type sequence I description CTP binding site source : CTB 2) chain B residue 17 type sequence V description CTP binding site source : CTB 3) chain B residue 19 type sequence D description CTP binding site source : CTB 4) chain B residue 60 type sequence K description CTP binding site source : CTB 5) chain B residue 84 type sequence N description CTP binding site source : CTB 6) chain B residue 89 type sequence Y description CTP binding site source : CTB 7) chain B residue 91 type sequence V description CTP binding site source : CTB 8) chain B residue 94 type sequence K description CTP binding site source : CTB 9) chain B residue 109 type sequence C description ZN binding site source : ZNB 10) chain B residue 114 type sequence C description ZN binding site source : ZNB 11) chain B residue 138 type sequence C description ZN binding site source : ZNB 12) chain B residue 141 type sequence C description ZN binding site source : ZNB 13) chain D residue 12 type sequence I description CTP binding site source : CTD 14) chain D residue 17 type sequence V description CTP binding site source : CTD 15) chain D residue 19 type sequence D description CTP binding site source : CTD 16) chain D residue 60 type sequence K description CTP binding site source : CTD 17) chain D residue 84 type sequence N description CTP binding site source : CTD 18) chain D residue 89 type sequence Y description CTP binding site source : CTD 19) chain D residue 91 type sequence V description CTP binding site source : CTD 20) chain D residue 94 type sequence K description CTP binding site source : CTD 21) chain D residue 109 type sequence C description ZN binding site source : ZND 22) chain D residue 114 type sequence C description ZN binding site source : ZND 23) chain D residue 138 type sequence C description ZN binding site source : ZND 24) chain D residue 141 type sequence C description ZN binding site source : ZND 25) chain B residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 26) chain B residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 27) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 28) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN B 154 source : AC1 29) chain D residue 109 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 30) chain D residue 114 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 31) chain D residue 138 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 32) chain D residue 141 type sequence C description BINDING SITE FOR RESIDUE ZN D 154 source : AC2 33) chain B residue 11 type sequence A description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 34) chain B residue 12 type sequence I description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 35) chain B residue 17 type sequence V description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 36) chain B residue 19 type sequence D description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 37) chain B residue 58 type sequence L description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 38) chain B residue 60 type sequence K description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 39) chain B residue 84 type sequence N description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 40) chain B residue 86 type sequence I description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 41) chain B residue 89 type sequence Y description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 42) chain B residue 91 type sequence V description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 43) chain B residue 94 type sequence K description BINDING SITE FOR RESIDUE CTP B 155 source : AC3 44) chain D residue 11 type sequence A description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 45) chain D residue 12 type sequence I description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 46) chain D residue 17 type sequence V description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 47) chain D residue 19 type sequence D description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 48) chain D residue 20 type sequence H description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 49) chain D residue 60 type sequence K description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 50) chain D residue 82 type sequence T description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 51) chain D residue 84 type sequence N description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 52) chain D residue 86 type sequence I description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 53) chain D residue 91 type sequence V description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 54) chain D residue 94 type sequence K description BINDING SITE FOR RESIDUE CTP D 155 source : AC4 55) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 56) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 57) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 58) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 59) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 60) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 61) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 62) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 63) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 64) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 65) chain B residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 66) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 67) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 68) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 69) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 70) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 71) chain B residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 72) chain B residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 73) chain B residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 74) chain D residue 109 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 75) chain D residue 114 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 76) chain D residue 138 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 77) chain D residue 141 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 78) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 79) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 80) 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 81) 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 82) 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 83) 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 84) 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 85) 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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