› 1rai

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY

Released:
DOI: 10.2210/pdb1rai/pdb
PDB entry 1rai coloured by chain, front view.
PDB entry 1rai coloured by chain, side view.
PDB entry 1rai coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity.
Kosman RP, Gouaux JE, Lipscomb WN
Proteins 15 147-76 (1993)
PMID: 8441751

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: 34.34 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided
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 K-12
Expression system: Not provided
UniProt:
  • Canonical: P0A7F3 (Residues: 1-153; Coverage: 100%)
Gene names: JW4203, b4244, pyrI
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand CTP 2 x CTP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P321
Unit cell:
a: 122.13Å b: 122.13Å c: 142.51Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.182 not available
Expression system: Not provided

Quick links

Citations

5 review citations

Artificial allosteric receptors.
Kremer et al. (2013)
4 more