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Crystal structure of fungal versatile peroxidase I from pleurotus ostreatus - crystal form V

Analyse Crystal structure of fungal versatile peroxidase I from pleurotus ostreatus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BLY
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.794
Source: PLEUROTUS OSTREATUS
Molecule: Versatile peroxidase I
EC: 1.11.1.16
Ligands: HEM, CA, SO4
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · resolution 1.794 · 1 distinct chain · 41% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Versatile peroxidase I (EC 1.11.1.16)	protein	329	41% helix, 8% strand	—

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CA · Calcium ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	409	0.81	0.89	46	HEM

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4BLY · Crystal structure of fungal versatile peroxidase I from pleurotus ostreatus - crystal… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 4BLY · PDBe 4BLY

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