› 5vnu

X-ray diffraction
1.58Å resolution

Nonheme Iron Replacement in a Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Mn-bound FeBMb

Released:
DOI: 10.2210/pdb5vnu/pdb
PDB entry 5vnu coloured by chain, front view.
PDB entry 5vnu coloured by chain, side view.
PDB entry 5vnu coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism.
Reed JH, Shi Y, Zhu Q, Chakraborty S, Mirts EN, Petrik ID, Bhagi-Damodaran A, Ross M, Moënne-Loccoz P, Zhang Y, Lu Y
J Am Chem Soc 139 12209-12218 (2017)
PMID: 28768416

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: 153 amino acids
Theoretical weight: 17.28 KDa
Source organism: Physeter catodon
Expression system: Escherichia coli
UniProt:
  • Canonical: P02185 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand HEM 1 x HEM
Ligand MN 1 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P212121
Unit cell:
a: 39.785Å b: 48.422Å c: 78.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.222
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.
Adam et al. (2018)
2 more

2 mentions without citation

Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism.
Reed et al. (2017)
1 more