› 3q6d

X-ray diffraction
1.97Å resolution

Xaa-Pro dipeptidase from Bacillus anthracis.

Released:
DOI: 10.2210/pdb3q6d/pdb
PDB entry 3q6d coloured by chain, front view.
PDB entry 3q6d coloured by chain, side view.
PDB entry 3q6d coloured by chain, top view.
Source organism: Bacillus anthracis str. Ames
Entry authors: Osipiuk J, Makowska-Grzyska M, Papazisi L, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
X-Pro dipeptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 356 amino acids
Theoretical weight: 38.93 KDa
Source organism: Bacillus anthracis str. Ames
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A6L7GZS1 (Residues: 1-353; Coverage: 100%)
Gene names: GBAA_4422, pepQ1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 59.502Å b: 107.912Å c: 252.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.247
Expression system: Escherichia coli BL21(DE3)

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