› 1xch

X-ray diffraction
1.7Å resolution

MYOGLOBIN (HORSE HEART) MUTANT WITH LEU 104 REPLACED BY ASN (L104N)

Released:
DOI: 10.2210/pdb1xch/pdb
PDB entry 1xch coloured by chain, front view.
PDB entry 1xch coloured by chain, side view.
PDB entry 1xch coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket.
Maurus R, Overall CM, Bogumil R, Luo Y, Mauk AG, Smith M, Brayer GD
Biochim Biophys Acta 1341 1-13 (1997)
PMID: 9300804

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-159278 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.98 KDa
Source organism: Equus caballus
Expression system: Escherichia coli
UniProt:
  • Canonical: P68082 (Residues: 2-154; Coverage: 99%)
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: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 64.566Å b: 28.872Å c: 35.882Å
α: 90° β: 107.17° γ: 90°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites.
Overall CM. (2002)
1 more

1 mention without citation

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