› 1bvd

X-ray diffraction
1.4Å resolution

STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K

Released:
DOI: 10.2210/pdb1bvd/pdb
PDB entry 1bvd coloured by chain, front view.
PDB entry 1bvd coloured by chain, side view.
PDB entry 1bvd coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution.
Wagner UG, Müller N, Schmitzberger W, Falk H, Kratky C
J Mol Biol 247 326-37 (1995)
PMID: 7707378

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135409 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 17.23 KDa
Source organism: Physeter catodon
UniProt:
  • Canonical: P02185 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

1 bound ligand:
Ligand BLA 1 x BLA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 39.799Å b: 50.604Å c: 74.651Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.259

Quick links

Citations

1 review citation

Structure and catalytic mechanism of heme oxygenase.
Unno et al. (2007)
18 other articles

3 mentions without citation

Sequence variations within protein families are linearly related to structural variations.
Koehl et al. (2002)
2 more