› 2kdx

Solution NMR

Solution structure of HypA protein

Released:
DOI: 10.2210/pdb2kdx/pdb
PDB entry 2kdx coloured by chain, ensemble of 20 models, front view.
PDB entry 2kdx coloured by chain, ensemble of 20 models, side view.
PDB entry 2kdx coloured by chain, ensemble of 20 models, top view.
Source organism: Helicobacter pylori 26695
Primary publication:
Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites.
Xia W, Li H, Sze KH, Sun H
J Am Chem Soc 131 10031-40 (2009)
PMID: 19621959

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydrogenase/urease maturation factor HypA Chain: A
Molecule details ›
Chain: A
Length: 119 amino acids
Theoretical weight: 13.37 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A0U4 (Residues: 1-117; Coverage: 100%)
Gene names: HP_0869, hypA
Sequence domains: Hydrogenase/urease nickel incorporation, metallochaperone, hypA
Structure domains: hypothetical protein PF0899 fold

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Insights into [FeFe]-hydrogenase structure, mechanism, and maturation.
Mulder et al. (2011)
9 more

7 mentions without citation

Specific metal recognition in nickel trafficking.
Higgins et al. (2012)
6 more