› 1qjs

X-ray diffraction
2.9Å resolution

mammalian blood serum haemopexin glycosylated-native protein and in complex with its ligand haem

Released:
DOI: 10.2210/pdb1qjs/pdb
PDB entry 1qjs coloured by chain, front view.
PDB entry 1qjs coloured by chain, side view.
PDB entry 1qjs 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 Chains: A, B
Molecule details ›
Chains: A, B
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 HEM 2 x HEM
Ligand PO4 2 x PO4
Ligand CL 4 x CL
Ligand NA 8 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 103.9Å b: 69.9Å c: 151.81Å
α: 90° β: 108.16° γ: 90°
R-values:
R R work R free
0.251 0.255 0.312

Quick links

Citations

45 review citations

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

7 mentions without citation

Heme Scavenging and Delivery: The Role of Human Serum Albumin.
De Simone et al. (2023)
6 more