› 3a54

X-ray diffraction
1.5Å resolution

Crystal structure of the A47Q1 mutant of pro-protein-glutaminase

Released:
DOI: 10.2210/pdb3a54/pdb
PDB entry 3a54 coloured by chain, front view.
PDB entry 3a54 coloured by chain, side view.
PDB entry 3a54 coloured by chain, top view.
Source organism: Chryseobacterium proteolyticum
Primary publication:
Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex.
Hashizume R, Maki Y, Mizutani K, Takahashi N, Matsubara H, Sugita A, Sato K, Yamaguchi S, Mikami B
J Biol Chem 286 38691-38702 (2011)
PMID: 21926168

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189599 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein glutaminase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 305 amino acids
Theoretical weight: 33.61 KDa
Source organism: Chryseobacterium proteolyticum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9AQQ8 (Residues: 22-320; Coverage: 100%)
Gene name: prgA
Sequence domains: Glutaminase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 56.986Å b: 104.113Å c: 134.189Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.14 0.167
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism.
Walsh et al. (2018)
1 more

4 mentions without citation

Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex.
Hashizume et al. (2011)
3 more