› 3o5v

X-ray diffraction
1.85Å resolution

The Crystal Structure of the Creatinase/Prolidase N-terminal domain of an X-PRO dipeptidase from Streptococcus pyogenes to 1.85A

Released:
DOI: 10.2210/pdb3o5v/pdb
PDB entry 3o5v coloured by chain, front view.
PDB entry 3o5v coloured by chain, side view.
PDB entry 3o5v coloured by chain, top view.
Source organism: Streptococcus pyogenes M1 GAS
Entry authors: Stein AJ, Wu R, Clancy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed: 
Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-189448 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
XAA-PRO dipeptidase X-PRO dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 132 amino acids
Theoretical weight: 15.05 KDa
Source organism: Streptococcus pyogenes M1 GAS
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9A119 (Residues: 3-131; Coverage: 36%)
Gene names: SPy_0513, pepQ
Sequence domains: Creatinase/Prolidase N-terminal domain
Structure domains: Creatinase/prolidase N-terminal domain

Ligands and Environments

2 bound ligands:
Ligand GOL 2 x GOL
Ligand CL 1 x CL
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 79.439Å b: 79.439Å c: 88.823Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.192 0.224
Expression system: Escherichia coli BL21(DE3)

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