› 2hse

X-ray diffraction
2.6Å resolution

Structure of D236A E. coli Aspartate Transcarbamoylase in the presence of phosphonoacetamide and l-Aspartate at 2.60 A resolution

Released:
DOI: 10.2210/pdb2hse/pdb
PDB entry 2hse coloured by chain, front view.
PDB entry 2hse coloured by chain, side view.
PDB entry 2hse coloured by chain, top view.
Source organism: Escherichia coli
Entry authors: Wang J, Kantrowitz ER

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141554 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate carbamoyltransferase catalytic subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 310 amino acids
Theoretical weight: 34.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A786 (Residues: 2-311; Coverage: 100%)
Gene names: JW4204, b4245, pyrB
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase
Aspartate carbamoyltransferase regulatory chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 153 amino acids
Theoretical weight: 17.14 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7F3 (Residues: 1-153; Coverage: 100%)
Gene names: JW4203, b4244, pyrI
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand PO4 1 x PO4
Ligand PCT 2 x PCT
Ligand ASP 3 x ASP
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P321
Unit cell:
a: 121.076Å b: 121.076Å c: 155.235Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.209 0.254
Expression system: Escherichia coli

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