› 1a7d

X-ray diffraction
1.8Å resolution

CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA

Released:
DOI: 10.2210/pdb1a7d/pdb
PDB entry 1a7d coloured by chain, front view.
PDB entry 1a7d coloured by chain, side view.
PDB entry 1a7d coloured by chain, top view.
Source organism: Themiste hennahi
Primary publication:
Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution.
Martins LJ, Hill CP, Ellis WR
Biochemistry 36 7044-9 (1997)
PMID: 9188702

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myohemerythrin Chain: A
Molecule details ›
Chain: A
Length: 118 amino acids
Theoretical weight: 13.8 KDa
Source organism: Themiste hennahi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02247 (Residues: 1-118; Coverage: 100%)
Sequence domains: Hemerythrin HHE cation binding domain
Structure domains: Hemerythrin-like

Ligands and Environments

2 bound ligands:
Ligand CL 2 x CL
Ligand CFO 1 x CFO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 41.842Å b: 81.26Å c: 36.831Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Internal sense of direction: sensing and signaling from cytoplasmic chemoreceptors.
Collins et al. (2014)
1 more

7 mentions without citation

Metal-binding dependent disruption of membranes by designed helices.
Signarvic et al. (2009)
6 more