› 5ojb

X-ray diffraction
1.54Å resolution

Structure of MbQ NMH

Released:
DOI: 10.2210/pdb5ojb/pdb
PDB entry 5ojb coloured by chain, front view.
PDB entry 5ojb coloured by chain, side view.
PDB entry 5ojb coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold.
Pott M, Hayashi T, Mori T, Mittl PRE, Green AP, Hilvert D
J Am Chem Soc 140 1535-1543 (2018)
PMID: 29309143

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

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: 163 amino acids
Theoretical weight: 18.38 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 HEM 1 x HEM
Ligand IMD 1 x IMD
1 modified residue:
Ligand MHS 1 x MHS

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P65
Unit cell:
a: 91.134Å b: 91.134Å c: 39.687Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.201 0.233
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Directed Evolution of Protein Catalysts.
Zeymer et al. (2018)
4 more

1 mention without citation

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