› 2at2

X-ray diffraction
3Å resolution

MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2at2/pdb
PDB entry 2at2 coloured by chain, front view.
PDB entry 2at2 coloured by chain, side view.
PDB entry 2at2 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution.
Stevens RC, Reinisch KM, Lipscomb WN
Proc Natl Acad Sci U S A 88 6087-91 (1991)
PMID: 1906175

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138728 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate carbamoyltransferase catalytic subunit Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 300 amino acids
Theoretical weight: 33.78 KDa
Source organism: Bacillus subtilis
Expression system: Not provided
UniProt:
  • Canonical: P05654 (Residues: 1-300; Coverage: 99%)
Gene names: BSU15490, pyrB
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 258.5Å b: 153.2Å c: 51.9Å
α: 90° β: 97.7° γ: 90°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Not provided

Quick links

Citations

3 review citations

Nucleotide metabolism and its control in lactic acid bacteria.
Kilstrup et al. (2005)
2 more

1 mention without citation

Crystallization and preliminary X-ray analysis of aspartate transcarbamoylase from the parasitic protist Trypanosoma cruzi.
Matoba et al. (2009)