› 3a54

X-ray diffraction
1.5Å resolution

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

Released:
DOI: 10.2210/pdb3a54/pdb
PDB 3a54 coloured by chain and viewed from the front.
PDB 3a54 coloured by chain and viewed from the side.
PDB 3a54 coloured by chain and viewed from the top.
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 38691-702 (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)
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

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Citations

1 review citation

Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism.
Walsh et al. (2018)
4 other articles

2 mentions without citation

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