eF-site ID 2at1-ABCD PDB Code 2at1 Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH 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 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) 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 22) 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 23) 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 24) 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 25) chain D residue 109 type sequence C description zn binding site source : ZND 26) chain D residue 114 type sequence C description zn binding site source : ZND 27) chain D residue 138 type sequence C description zn binding site source : ZND 28) chain D residue 141 type sequence C description zn binding site source : ZND 29) chain A residue 55 type catalytic sequence T description 405 source MCSA : MCSA1 30) chain A residue 56 type catalytic sequence R description 405 source MCSA : MCSA1 31) chain A residue 85 type catalytic sequence G description 405 source MCSA : MCSA1 32) chain A residue 106 type catalytic sequence H description 405 source MCSA : MCSA1 33) chain A residue 135 type catalytic sequence P description 405 source MCSA : MCSA1 34) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 35) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 36) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 37) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 38) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 39) chain A residue 48-55 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 40) chain B residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 41) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 42) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 43) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 44) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 45) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 46) chain B residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 47) chain B residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 48) chain B residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 49) chain D residue 110 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 50) chain D residue 115 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 51) chain D residue 139 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 52) chain D residue 142 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 53) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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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