› 1nz4

X-ray diffraction
1.8Å resolution

The horse heart myoglobin variant K45E/K63E complexed with Cadmium

Released:
DOI: 10.2210/pdb1nz4/pdb
PDB entry 1nz4 coloured by chain, front view.
PDB entry 1nz4 coloured by chain, side view.
PDB entry 1nz4 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Introduction and characterization of a functionally linked metal ion binding site at the exposed heme edge of myoglobin.
Hunter CL, Maurus R, Mauk MR, Lee H, Raven EL, Tong H, Nguyen N, Smith M, Brayer GD, Mauk AG
Proc Natl Acad Sci U S A 100 3647-52 (2003)
PMID: 12644706

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 CD 2 x CD
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 29.3Å b: 35.8Å c: 125.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 not available not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Rational heme protein design: all roads lead to Rome.
Lin et al. (2013)
8 other articles

1 mention without citation

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