› 3azq

X-ray diffraction
2.7Å resolution

Crystal structure of puromycin hydrolase S511A mutant complexed with PGG

Released:
DOI: 10.2210/pdb3azq/pdb
PDB entry 3azq coloured by chain, front view.
PDB entry 3azq coloured by chain, side view.
PDB entry 3azq coloured by chain, top view.
Source organism: Streptomyces morookaense
Primary publication:
Structural evidence that puromycin hydrolase is a new type of aminopeptidase with a prolyl oligopeptidase family fold.
Matoba Y, Nakayama A, Oda K, Noda M, Kumagai T, Nishimura M, Sugiyama M
Proteins 79 2999-3005 (2011)
PMID: 21905123

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163427 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 662 amino acids
Theoretical weight: 71.27 KDa
Source organism: Streptomyces morookaense
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2HXD9 (Residues: 1-662; Coverage: 100%)
Gene name: HG542_00635
Sequence domains: Prolyl oligopeptidase family
Structure domains: alpha/beta hydrolase
tripeptide PGG Chains: C, D
Molecule details ›
Chains: C, D
Length: 3 amino acids
Theoretical weight: 229 Da
Source organism: Streptomyces morookaense
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 10 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 84.43Å b: 142.68Å c: 156.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.24
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 citation in other articles

A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.
Brocca et al. (2016)
2 more

2 mentions without citation

Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates.
Chekan et al. (2016)
1 more