› 1cp5

X-ray diffraction
2.1Å resolution

RECOMBINANT SPERM WHALE MYOGLOBIN L104F MUTANT (MET)

Released:
DOI: 10.2210/pdb1cp5/pdb
PDB entry 1cp5 coloured by chain, front view.
PDB entry 1cp5 coloured by chain, side view.
PDB entry 1cp5 coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Waterproofing the heme pocket. Role of proximal amino acid side chains in preventing hemin loss from myoglobin.
Liong EC, Dou Y, Scott EE, Olson JS, Phillips GN
J Biol Chem 276 9093-100 (2001)
PMID: 11084036

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: 154 amino acids
Theoretical weight: 17.4 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

2 bound ligands:
Ligand SO4 1 x SO4
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P6
Unit cell:
a: 91.6Å b: 91.6Å c: 45.904Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.147 not available 0.208
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structure and reactivity of hexacoordinate hemoglobins.
Kakar et al. (2010)
3 more

1 mention without citation

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