Research workbench

F194W mutant of the dye-decolorizing peroxidase (dyp) from pleurotus ostreatus

Analyse F194W mutant of the dye-decolorizing peroxidase (dyp) 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: 6FSL
Type: protein
Length: 968 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dyp-type peroxidase
UniProt: A0A067N4E7
Ligands: HEM
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dyp-type peroxidase	protein	484	31% helix, 19% strand	A0A067N4E7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	751	0.81	0.84	85	HEM
2	768	0.80	0.84	86	HEM
3	883	0.75	0.79	62	empty
4	232	0.53	0.77	35	empty

Interfaces

1 interface between chains.

A–B · 669 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6FSL · F194W mutant of the dye-decolorizing peroxidase (DYP) from Pleurotus ostreatus · 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
Every structure of UniProt A0A067N4E7
Elsewhere: RCSB PDB 6FSL · PDBe 6FSL · UniProt A0A067N4E7

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