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Trametes cervina lignin peroxidase

Analyse Trametes cervina lignin peroxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q3U
Type: protein
Length: 338 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lignin peroxidase
UniProt: Q60FD2
Ligands: HEM, CA, NA, CL
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lignin peroxidase	protein	338	43% helix, 8% strand	Q60FD2

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CA · Calcium ion · metal · 2 copies · chains A
NA · Sodium ion · metal
CL · Chloride ion · ion · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	389	0.81	0.90	43	HEM
2	63	0.30	0.75	26	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3Q3U · Trametes cervina lignin peroxidase · 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 Q60FD2
Elsewhere: RCSB PDB 3Q3U · PDBe 3Q3U · UniProt Q60FD2

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