› 6sre

X-ray diffraction
1.39Å resolution

Crystal Structure of Human Prolidase S202F variant expressed in the presence of chaperones

Released:
DOI: 10.2210/pdb6sre/pdb
PDB entry 6sre coloured by chain, front view.
PDB entry 6sre coloured by chain, side view.
PDB entry 6sre coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Co-expression with chaperones can affect protein 3D structure as exemplified by loss-of-function variants of human prolidase.
Wątor E, Rutkiewicz M, Weiss MS, Wilk P
FEBS Lett 594 3045-3056 (2020)
PMID: 32598484

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-146399 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 484 amino acids
Theoretical weight: 53.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P12955 (Residues: 6-489; Coverage: 98%)
Gene names: PEPD, PRD
Sequence domains:

Ligands and Environments

5 bound ligands:
Ligand MN 2 x MN
Ligand GOL 9 x GOL
Ligand MH2 2 x MH2
Ligand GLY 2 x GLY
Ligand PRO 2 x PRO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 103.725Å b: 106.858Å c: 216.323Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.15 0.172
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

G-quadruplexes rescuing protein folding.
Son et al. (2023)
1 more

1 mention without citation

Co-expression with chaperones can affect protein 3D structure as exemplified by loss-of-function variants of human prolidase.
Wątor et al. (2020)