› 3nu1

X-ray diffraction
2.5Å resolution

Structure of holo form of a periplasmic heme binding protein

Released:
DOI: 10.2210/pdb3nu1/pdb
PDB entry 3nu1 coloured by chain, front view.
PDB entry 3nu1 coloured by chain, side view.
PDB entry 3nu1 coloured by chain, top view.
Source organism: Yersinia pestis Antiqua
Primary publication:
Two stacked heme molecules in the binding pocket of the periplasmic heme-binding protein HmuT from Yersinia pestis.
Mattle D, Zeltina A, Woo JS, Goetz BA, Locher KP
J Mol Biol 404 220-31 (2010)
PMID: 20888343

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101178 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fe/B12 periplasmic-binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 254 amino acids
Theoretical weight: 26.84 KDa
Source organism: Yersinia pestis Antiqua
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0E1NWS3 (Residues: 26-279; Coverage: 100%)
Gene name: YPA_4001
Sequence domains: Periplasmic binding protein
Structure domains: Nitrogenase molybdenum iron protein domain

Ligands and Environments

1 bound ligand:
Ligand HEM 4 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P6122
Unit cell:
a: 89.24Å b: 89.24Å c: 288.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.238
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Recent insights into iron import by bacteria.
Braun et al. (2011)
11 more

3 mentions without citation

Bacterial iron detoxification at the molecular level.
Bradley et al. (2020)
2 more