› 3e2p

X-ray diffraction
3Å resolution

Catalytic subunit of M. Jannaschii aspartate transcarbamoylase in an orthorhombic crystal form

Released:
DOI: 10.2210/pdb3e2p/pdb
PDB entry 3e2p coloured by chain, front view.
PDB entry 3e2p coloured by chain, side view.
PDB entry 3e2p coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form.
Vitali J, Colaneri MJ
Acta Crystallogr Sect F Struct Biol Cryst Commun 64 776-80 (2008)
PMID: 18765902

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

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-176721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate carbamoyltransferase catalytic subunit Chains: A, B, C, D, E, F, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, I, J, K, L, M, N
Length: 306 amino acids
Theoretical weight: 35.21 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58976 (Residues: 1-306; Coverage: 100%)
Gene names: MJ1581, pyrB
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P212121
Unit cell:
a: 87.13Å b: 167.93Å c: 319.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.269
Expression system: Escherichia coli

Quick links

Citations

1 review citation

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases.
Shi et al. (2015)

1 mention without citation

Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form.
Vitali et al. (2008)