eF-site ID 7at1-ABCD PDB Code 7at1 Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL P*H Classification TRANSFERASE (CARBAMOYL-P,ASPARTATE) Compound ASPARTATE CARBAMOYLTRANSFERASE (R 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 A residue 54 type sequence R description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 2) chain A residue 55 type sequence T description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 3) chain A residue 105 type sequence R description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 4) chain A residue 134 type sequence H description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 5) chain A residue 137 type sequence Q description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 6) chain A residue 167 type sequence R description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 7) chain A residue 229 type sequence R description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 8) chain A residue 231 type sequence Q description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 9) chain A residue 266 type sequence P description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 10) chain A residue 267 type sequence L description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMA 11) chain B residue 109 type sequence C description zn binding site source : ZNB 12) chain B residue 114 type sequence C description zn binding site source : ZNB 13) chain B residue 138 type sequence C description zn binding site source : ZNB 14) chain B residue 141 type sequence C description zn binding site source : ZNB 15) chain B residue 8 type sequence G description ALLOSTERIC BINDING SITE source : ATB 16) chain B residue 9 type sequence V description ALLOSTERIC BINDING SITE source : ATB 17) chain B residue 10 type sequence E description ALLOSTERIC BINDING SITE source : ATB 18) chain B residue 11 type sequence A description ALLOSTERIC BINDING SITE source : ATB 19) chain B residue 12 type sequence I description ALLOSTERIC BINDING SITE source : ATB 20) chain B residue 19 type sequence D description ALLOSTERIC BINDING SITE source : ATB 21) chain B residue 20 type sequence H description ALLOSTERIC BINDING SITE source : ATB 22) chain B residue 56 type sequence K description ALLOSTERIC BINDING SITE source : ATB 23) chain B residue 60 type sequence K description ALLOSTERIC BINDING SITE source : ATB 24) chain B residue 84 type sequence N description ALLOSTERIC BINDING SITE source : ATB 25) chain B residue 89 type sequence Y description ALLOSTERIC BINDING SITE source : ATB 26) chain B residue 94 type sequence K description ALLOSTERIC BINDING SITE source : ATB 27) chain C residue 54 type sequence R description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 28) chain C residue 55 type sequence T description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 29) chain C residue 105 type sequence R description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 30) chain C residue 134 type sequence H description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 31) chain C residue 137 type sequence Q description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 32) chain C residue 167 type sequence R description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 33) chain C residue 229 type sequence R description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 34) chain C residue 231 type sequence Q description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 35) chain C residue 266 type sequence P description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 36) chain C residue 267 type sequence L description BINDING SITES OF COMBINED *PCT* AND *MAL* MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN. source : PMC 37) chain D residue 109 type sequence C description zn binding site source : ZND 38) chain D residue 114 type sequence C description zn binding site source : ZND 39) chain D residue 138 type sequence C description zn binding site source : ZND 40) chain D residue 141 type sequence C description zn binding site source : ZND 41) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 42) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 43) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 44) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 45) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 46) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 47) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 48) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 49) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 50) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 51) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 52) chain B residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 53) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 54) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 55) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 56) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 57) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 58) chain B residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 59) chain B residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 60) chain B residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 61) chain D residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 62) chain D residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 63) chain D residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 64) chain D residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 65) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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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