› 1ly8

X-ray diffraction
2.05Å resolution

The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures

Released:
DOI: 10.2210/pdb1ly8/pdb
PDB entry 1ly8 coloured by chain, front view.
PDB entry 1ly8 coloured by chain, side view.
PDB entry 1ly8 coloured by chain, top view.
Source organism: Coprinopsis cinerea
Primary publication:
The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability.
Houborg K, Harris P, Poulsen JC, Schneider P, Svendsen A, Larsen S
Acta Crystallogr D Biol Crystallogr 59 997-1003 (2003)
PMID: 12777761

Function and Biology Details

Reaction catalysed: 
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 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-151201 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 35.48 KDa
Source organism: Coprinopsis cinerea
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P28314 (Residues: 21-363; Coverage: 100%)
Gene name: CIP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
5 bound ligands:
Ligand NAG 2 x NAG
Ligand BMA 2 x BMA
Ligand MAN 2 x MAN
Ligand CA 4 x CA
Ligand GOL 12 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21212
Unit cell:
a: 74.49Å b: 114.86Å c: 73.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.249
Expression system: Saccharomyces cerevisiae

Quick links

Citations

1 review citation

New and classic families of secreted fungal heme peroxidases.
Hofrichter et al. (2010)
2 other articles