› 1duk

X-ray diffraction
2.13Å resolution

WILD-TYPE RECOMBINANT SPERM WHALE METAQUOMYOGLOBIN

Released:
DOI: 10.2210/pdb1duk/pdb
PDB entry 1duk coloured by chain, front view.
PDB entry 1duk coloured by chain, side view.
PDB entry 1duk coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Trans-substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletion.
Barrick D, Dahlquist FW
Proteins 39 278-90 (2000)
PMID: 10813811

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
Expression system: Escherichia coli
UniProt:
  • Canonical: P02185 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 40.132Å b: 49.071Å c: 79.339Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 not available not available
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme.
Kundu et al. (2002)
4 more

3 mentions without citation

Imaging the migration pathways for O2, CO, NO, and Xe inside myoglobin.
Cohen et al. (2006)
2 more