› 5vmq

X-ray diffraction
2.01Å resolution

STRUCTURE OF THE R105A MUTANT CATALYTIC TRIMER OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE AT 2.0-A RESOLUTION

Released:
DOI: 10.2210/pdb5vmq/pdb
PDB entry 5vmq coloured by chain, front view.
PDB entry 5vmq coloured by chain, side view.
PDB entry 5vmq coloured by chain, top view.
Source organism: Escherichia coli S88
Primary publication:
Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
Endrizzi JA, Beernink PT
Protein Sci 26 2221-2228 (2017)
PMID: 28833948

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate carbamoyltransferase catalytic subunit Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 310 amino acids
Theoretical weight: 34.25 KDa
Source organism: Escherichia coli S88
Expression system: Escherichia coli
UniProt:
  • Canonical: B7MLQ3 (Residues: 2-311; Coverage: 100%)
Gene names: ECS88_4835, pyrB
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 56.03Å b: 81.1Å c: 211.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.227
Expression system: Escherichia coli

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Citations

2 mentions without citation

Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
Endrizzi et al. (2017)
1 more