› 1ouv

X-ray diffraction
2Å resolution

Helicobacter cysteine rich protein C (HcpC)

Released:
DOI: 10.2210/pdb1ouv/pdb
PDB entry 1ouv coloured by chain, front view.
PDB entry 1ouv coloured by chain, side view.
PDB entry 1ouv coloured by chain, top view.
Source organism: Helicobacter pylori 26695
Primary publication:
The crystal structure of Helicobacter cysteine-rich protein C at 2.0 A resolution: similar peptide-binding sites in TPR and SEL1-like repeat proteins.
Lüthy L, Grütter MG, Mittl PR
J Mol Biol 340 829-41 (2004)
PMID: 15223324

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative beta-lactamase HcpC Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 29.97 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O25728 (Residues: 24-290; Coverage: 100%)
Gene names: HP_1098, hcpC
Sequence domains: Sel1 repeat
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: C2
Unit cell:
a: 102.982Å b: 46.198Å c: 76.39Å
α: 90° β: 120.95° γ: 90°
R-values:
R R work R free
0.225 0.202 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Sel1-like repeat proteins in signal transduction.
Mittl et al. (2007)
2 more

15 mentions without citation

Structural and functional aspects of the Helicobacter pylori secretome.
Zanotti et al. (2014)
14 more