› 1gxu

X-ray diffraction
1.27Å resolution

Hydrogenase Maturation Protein HypF "acylphosphatase-like" N-terminal domain (HypF-ACP) in complex with a substrate. Crystal grown in the presence of carbamoylphosphate

Released:
DOI: 10.2210/pdb1gxu/pdb
PDB entry 1gxu coloured by chain, front view.
PDB entry 1gxu coloured by chain, side view.
PDB entry 1gxu coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain.
Rosano C, Zuccotti S, Bucciantini M, Stefani M, Ramponi G, Bolognesi M
J Mol Biol 321 785-96 (2002)
PMID: 12206761

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151648 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbamoyltransferase HypF Chain: A
Molecule details ›
Chain: A
Length: 91 amino acids
Theoretical weight: 10.4 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P30131 (Residues: 1-91; Coverage: 12%)
Gene names: JW5433, b2712, hydA, hypF
Sequence domains: Acylphosphatase
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand 2HP 1 x 2HP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: R32
Unit cell:
a: 57.994Å b: 57.994Å c: 156.414Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.133 0.131 0.161
Expression system: Not provided

Quick links

Citations

5 review citations

Nickel uptake and utilization by microorganisms.
Mulrooney et al. (2003)
4 more

15 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
14 more