PDBe 1m6v

X-ray diffraction
2.1Å resolution

Crystal Structure of the G359F (small subunit) Point Mutant of Carbamoyl Phosphate Synthetase

Released:
Source organism: Escherichia coli
Primary publication:
Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia.
J. Biol. Chem. 277 39722-7 (2002)
PMID: 12130656

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carbamoyl-phosphate synthase large chain Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 1073 amino acids
Theoretical weight: 117.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00968 (Residues: 1-1073; Coverage: 100%)
Gene names: JW0031, b0033, carB, pyrA
Sequence domains:
Structure domains:
Carbamoyl-phosphate synthase small chain Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 382 amino acids
Theoretical weight: 41.57 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F1 (Residues: 1-382; Coverage: 100%)
Gene names: JW0030, b0032, carA, pyrA
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 151.5Å b: 164.2Å c: 331.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.174 0.245
Expression system: Escherichia coli