› 1mn2

X-ray diffraction
2Å resolution

MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT E35Q, D179N

Released:
DOI: 10.2210/pdb1mn2/pdb
PDB entry 1mn2 coloured by chain, front view.
PDB entry 1mn2 coloured by chain, side view.
PDB entry 1mn2 coloured by chain, top view.
Source organism: Phanerodontia chrysosporium
Primary publication:
Crystal structures of substrate binding site mutants of manganese peroxidase.
Sundaramoorthy M, Kishi K, Gold MH, Poulos TL
J Biol Chem 272 17574-80 (1997)
PMID: 9211904

Function and Biology Details

Reaction catalysed: 
2 Mn(2+) + 2 H(+) + H(2)O(2) = 2 Mn(3+) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169732 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Manganese peroxidase 1 Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 37.48 KDa
Source organism: Phanerodontia chrysosporium
Expression system: Phanerodontia chrysosporium
UniProt:
  • Canonical: Q02567 (Residues: 22-378; Coverage: 100%)
Gene name: MNP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: C2
Unit cell:
a: 163.24Å b: 45.97Å c: 53.57Å
α: 90° β: 97.16° γ: 90°
R-values:
R R work R free
0.187 0.187 not available
Expression system: Phanerodontia chrysosporium

Quick links

Citations

12 review citations

Microbial biodegradation of polyaromatic hydrocarbons.
Peng et al. (2008)
11 more

2 mentions without citation

Reducing the computational complexity of protein folding via fragment folding and assembly.
Haspel et al. (2003)
1 more