› 1bvc

X-ray diffraction
1.5Å resolution

STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM D) AT 118 K

Released:
DOI: 10.2210/pdb1bvc/pdb
PDB entry 1bvc coloured by chain, front view.
PDB entry 1bvc coloured by chain, side view.
PDB entry 1bvc 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

2 bound ligands:
Ligand PO4 4 x PO4
Ligand BLA 1 x BLA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 33.653Å b: 58.863Å c: 76.379Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 not available

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Citations

1 review citation

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

16 mentions without citation

Statistical coil model of the unfolded state: resolving the reconciliation problem.
Jha et al. (2005)
15 more