› 4qr8

X-ray diffraction
2Å resolution

Crystal Structure of E coli pepQ

Released:
DOI: 10.2210/pdb4qr8/pdb
PDB entry 4qr8 coloured by chain, front view.
PDB entry 4qr8 coloured by chain, side view.
PDB entry 4qr8 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural basis of substrate selectivity of E. coli prolidase.
Weaver J, Watts T, Li P, Rye HS
PLoS One 9 e111531 (2014)
PMID: 25354344

Function and Biology Details

Reaction catalysed: 
Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149119 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 443 amino acids
Theoretical weight: 50.23 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P21165 (Residues: 1-443; Coverage: 100%)
Gene names: JW3823, b3847, pepQ
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 72.569Å b: 97.44Å c: 126.936Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.211
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.
Lyagin et al. (2021)
7 other articles

2 mentions without citation

GroEL actively stimulates folding of the endogenous substrate protein PepQ.
Weaver et al. (2017)
1 more