eF-site ID 7at1-C PDB Code 7at1 Chain C 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 C:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL Description Functional site 1) 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 2) 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 3) 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 4) 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 5) 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 6) 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 7) 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 8) 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 9) 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 10) 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 11) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 12) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 13) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 14) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 15) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 16) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 17) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 18) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 19) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 20) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 21) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 22) 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 23) 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 24) 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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