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Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii

Analyse Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FIM
Type: protein
Length: 565 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aryl-alcohol oxidase
EC: 1.1.3.7
UniProt: O94219
Ligands: FAD
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Aryl-alcohol oxidase (EC 1.1.3.7)	protein	565	31% helix, 21% strand	O94219

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	559	0.84	0.90	88	FAD
2	60	0.30	0.74	15	empty
3	57	0.28	0.75	18	empty
4	51	0.27	0.74	11	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3FIM · Crystal structure of aryl-alcohol-oxidase from Pleurotus eryingii · the same entry in another collection · chain B against B, 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 O94219
Elsewhere: RCSB PDB 3FIM · PDBe 3FIM · UniProt O94219

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