› 1do3

X-ray diffraction
1.55Å resolution

CARBONMONOXY-MYOGLOBIN (MUTANT L29W) AFTER PHOTOLYSIS AT T>180K

Released:
DOI: 10.2210/pdb1do3/pdb
PDB entry 1do3 coloured by chain, front view.
PDB entry 1do3 coloured by chain, side view.
PDB entry 1do3 coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Ligand binding and conformational motions in myoglobin.
Ostermann A, Waschipky R, Parak FG, Nienhaus GU
Nature 404 205-8 (2000)
PMID: 10724176

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
Macromolecules (2 distinct):
Myoglobin Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 17.47 KDa
Source organism: Physeter catodon
Expression system: Escherichia coli
UniProt:
  • Canonical: P02185 (Residues: 1-154; Coverage: 100%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
3 bound ligands:
Ligand SO4 2 x SO4
Ligand HEM 1 x HEM
Ligand CMO 1 x CMO
1 modified residue:
Ligand FME 1 x FME

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P6
Unit cell:
a: 90.46Å b: 90.46Å c: 45.26Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.193 0.218
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Transition networks for modeling the kinetics of conformational change in macromolecules.
Noé et al. (2008)
16 more

2 mentions without citation

Complex of myoglobin with phenol bound in a proximal cavity.
Huang et al. (2012)
1 more