› 2hmz

X-ray diffraction
1.66Å resolution

THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2hmz/pdb
PDB entry 2hmz coloured by chain, front view.
PDB entry 2hmz coloured by chain, side view.
PDB entry 2hmz coloured by chain, top view.
Source organism: Themiste dyscritum
Primary publication:
Structures of met and azidomet hemerythrin at 1.66 A resolution.
Holmes MA, Stenkamp RE
J Mol Biol 220 723-37 (1991)
PMID: 1870128

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: 13.35 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

2 bound ligands:
Ligand ACT 4 x ACT
Ligand FEA 4 x FEA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P4
Unit cell:
a: 86.6Å b: 86.6Å c: 80.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 not available not available
Expression system: Not provided

Quick links

Citations

5 review citations

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

3 mentions without citation

Do all backbone polar groups in proteins form hydrogen bonds?
Fleming et al. (2005)
2 more