› 2blj

X-ray diffraction
1.8Å resolution

Structure of L29W MbCO

Released:
DOI: 10.2210/pdb2blj/pdb
PDB entry 2blj coloured by chain, front view.
PDB entry 2blj coloured by chain, side view.
PDB entry 2blj coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Ligand migration and protein fluctuations in myoglobin mutant L29W.
Nienhaus K, Ostermann A, Nienhaus GU, Parak FG, Schmidt M
Biochemistry 44 5095-105 (2005)
PMID: 15794647

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: M
Molecule details ›
Chain: M
Length: 153 amino acids
Theoretical weight: 17.31 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

2 bound ligands:
Ligand HEM 1 x HEM
Ligand CMO 1 x CMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P6
Unit cell:
a: 91.87Å b: 91.87Å c: 46.04Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.224 0.257
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Advances in kinetic protein crystallography.
Bourgeois et al. (2005)
2 more

1 mention without citation

Water stabilizes an alternate turn conformation in horse heart myoglobin.
Bronstein et al. (2023)