› 1lyc

X-ray diffraction
1.57Å resolution

The impact of the physical and chemical enviroment on the molecular structure of Coprinus cinereus peroxidase

Released:
DOI: 10.2210/pdb1lyc/pdb
PDB entry 1lyc coloured by chain, front view.
PDB entry 1lyc coloured by chain, side view.
PDB entry 1lyc coloured by chain, top view.
Source organism: Coprinopsis cinerea
Primary publication:
Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase.
Houborg K, Harris P, Petersen J, Rowland P, Poulsen JC, Schneider P, Vind J, Larsen S
Acta Crystallogr D Biol Crystallogr 59 989-96 (2003)
PMID: 12777760

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: 35.58 KDa
Source organism: Coprinopsis cinerea
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: P28314 (Residues: 21-363; Coverage: 100%)
Gene name: CIP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B, RIGAKU
Spacegroup: P21
Unit cell:
a: 77.289Å b: 115.055Å c: 36.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.223 0.265
Expression system: Aspergillus oryzae

Quick links

Citations

9 citation in other articles

Solvated docking: introducing water into the modelling of biomolecular complexes.
van Dijk et al. (2006)
8 more

1 mention without citation

Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.
Smith et al. (2009)