› 1wvp

X-ray diffraction
1.53Å resolution

Structure of chemically modified myoglobin with distal N-tetrazolyl-histidine E7(64)

Released:
DOI: 10.2210/pdb1wvp/pdb
PDB entry 1wvp coloured by chain, front view.
PDB entry 1wvp coloured by chain, side view.
PDB entry 1wvp coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Heme environmental structure of a novel artificial myoglobin with a closed heme pocket: site-specific chemical modification producing distal N-tetrazolylhistidine E7 by cyanogen bromide and azide ion
Kamiya N, Shiro Y, Iwata T, Iizuka T, Iwasaki H
J. Am. Chem. Soc. 113 1826-1829 (1991)

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: 153 amino acids
Theoretical weight: 17.29 KDa
Source organism: Physeter catodon
UniProt:
  • Canonical: P02185 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand HEM 1 x HEM
1 modified residue:
Ligand NZH 1 x NZH

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P43212
Unit cell:
a: 60.982Å b: 60.982Å c: 84.808Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.208

Quick links

Citations

1 mention without citation

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