› 4hvt

X-ray diffraction
1.7Å resolution

Structure of a Post-proline cleaving enzyme from Rickettsia typhi

Released:
DOI: 10.2210/pdb4hvt/pdb
PDB entry 4hvt coloured by chain, front view.
PDB entry 4hvt coloured by chain, side view.
PDB entry 4hvt coloured by chain, top view.
Source organism: Rickettsia typhi str. Wilmington
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed: 
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179358 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Post-proline cleaving enzyme Chain: A
Molecule details ›
Chain: A
Length: 711 amino acids
Theoretical weight: 82.23 KDa
Source organism: Rickettsia typhi str. Wilmington
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q68XJ3 (Residues: 19-720; Coverage: 98%)
Gene names: RT0165, ppcE
Sequence domains:
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand EDO 6 x EDO
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1, RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 199.59Å b: 73.28Å c: 55.46Å
α: 90° β: 98.52° γ: 90°
R-values:
R R work R free
0.172 0.17 0.209
Expression system: Escherichia coli BL21(DE3)

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