› 2in4

X-ray diffraction
2.15Å resolution

Crystal Structure of Myoglobin with Charge Neutralized Heme, ZnDMb-dme

Released:
DOI: 10.2210/pdb2in4/pdb
PDB 2in4 coloured by chain and viewed from the front.
PDB 2in4 coloured by chain and viewed from the side.
PDB 2in4 coloured by chain and viewed from the top.
Source organism: Equus caballus
Primary publication:
Dynamic docking of cytochrome b5 with myoglobin and alpha-hemoglobin: heme-neutralization "squares" and the binding of electron-transfer-reactive configurations.
Wheeler KE, Nocek JM, Cull DA, Yatsunyk LA, Rosenzweig AC, Hoffman BM
J. Am. Chem. Soc. 129 3906-17 (2007)
PMID: 17343378

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (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
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 HE5 1 x HE5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 42.604Å b: 30.577Å c: 56.485Å
α: 90° β: 97.66° γ: 90°
R-values:
R R work R free
0.178 0.175 0.232

Quick links

Citations

7 review citations

The role of globins in cardiovascular physiology.
Keller et al. (2022)
6 more

1 mention without citation

Factors correlating with significant differences between X-ray structures of myoglobin.
Rashin et al. (2014)