› 1qhu

X-ray diffraction
2.3Å resolution

MAMMALIAN BLOOD SERUM HAEMOPEXIN DEGLYCOSYLATED AND IN COMPLEX WITH ITS LIGAND HAEM

Released:
DOI: 10.2210/pdb1qhu/pdb
PDB entry 1qhu coloured by chain, front view.
PDB entry 1qhu coloured by chain, side view.
PDB entry 1qhu coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains.
Paoli M, Anderson BF, Baker HM, Morgan WT, Smith A, Baker EN
Nat Struct Biol 6 926-31 (1999)
PMID: 10504726

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148826 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemopexin Chain: A
Molecule details ›
Chain: A
Length: 460 amino acids
Theoretical weight: 51.83 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P20058 (Residues: 1-460; Coverage: 100%)
Gene name: HPX
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain

Ligands and Environments

4 bound ligands:
Ligand CL 2 x CL
Ligand NA 4 x NA
Ligand PO4 1 x PO4
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 44.68Å b: 61.95Å c: 83.29Å
α: 90° β: 93.21° γ: 90°
R-values:
R R work R free
0.201 0.207 0.289

Quick links

Citations

45 review citations

Mechanisms of cell protection by heme oxygenase-1.
Gozzelino et al. (2010)
44 more

11 mentions without citation

Iron Metabolism at the Interface between Host and Pathogen: From Nutritional Immunity to Antibacterial Development.
Marchetti et al. (2020)
10 more