› 1hmo

X-ray diffraction
2Å resolution

THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1hmo/pdb
PDB entry 1hmo coloured by chain, front view.
PDB entry 1hmo coloured by chain, side view.
PDB entry 1hmo coloured by chain, top view.
Source organism: Themiste dyscritum
Primary publication:
Structures of deoxy and oxy hemerythrin at 2.0 A resolution.
Holmes MA, Le Trong I, Turley S, Sieker LC, Stenkamp RE
J Mol Biol 218 583-93 (1991)
PMID: 2016748

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo octamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135427 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemerythrin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 113 amino acids
Theoretical weight: 13.37 KDa
Source organism: Themiste dyscritum
Expression system: Not provided
UniProt:
  • Canonical: P02246 (Residues: 1-113; Coverage: 100%)
Sequence domains: Hemerythrin HHE cation binding domain
Structure domains: Hemerythrin-like

Ligands and Environments

3 bound ligands:
Ligand ACE 4 x ACE
Ligand FEO 4 x FEO
Ligand OXY 4 x OXY
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P4
Unit cell:
a: 86.69Å b: 86.69Å c: 80.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 not available not available
Expression system: Not provided

Quick links

Citations

7 review citations

Di-iron-carboxylate proteins.
Nordlund et al. (1995)
6 more

3 mentions without citation

Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.
Jasniewski et al. (2018)
2 more