› 1dkh

X-ray diffraction
3.2Å resolution

CRYSTAL STRUCTURE OF THE HEMOPHORE HASA, PH 6.5

Released:
DOI: 10.2210/pdb1dkh/pdb
PDB entry 1dkh coloured by chain, front view.
PDB entry 1dkh coloured by chain, side view.
PDB entry 1dkh coloured by chain, top view.
Source organism: Serratia marcescens
Primary publication:
Functional aspects of the heme bound hemophore HasA by structural analysis of various crystal forms.
Arnoux P, Haser R, Izadi-Pruneyre N, Lecroisey A, Czjzek M
Proteins 41 202-10 (2000)
PMID: 10966573

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176203 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemophore HasA Chain: A
Molecule details ›
Chain: A
Length: 188 amino acids
Theoretical weight: 19.29 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54450 (Residues: 1-188; Coverage: 100%)
Gene name: hasA
Sequence domains: Heme-binding protein A (HasA)
Structure domains: Haem-binding HasA

Ligands and Environments

3 bound ligands:
Ligand ZN 3 x ZN
Ligand SM 1 x SM
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 111.65Å b: 111.65Å c: 52.79Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.228 0.288
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.
Anzaldi et al. (2010)
4 more

2 mentions without citation

Iron Acquisition in Mycobacterium tuberculosis.
Chao et al. (2019)
1 more