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Cholesterol oxidase from streptomyces GLU361GLN mutant

Analyse Cholesterol oxidase from streptomyces GLU361GLN mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B8S
Type: protein
Length: 498 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (cholesterol oxidase)
EC: 1.1.3.6
UniProt: P12676
Ligands: FAD
Pockets: 3 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (cholesterol oxidase) (EC 1.1.3.6)	protein	498	29% helix, 25% strand	P12676

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

3 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	739	0.86	0.89	87	FAD
2	125	0.41	0.76	23	empty
3	81	0.32	0.74	25	empty

Compared structures

1B8S · Cholesterol oxidase from streptomyces GLU361GLN mutant · the same entry in another collection · chain A against A, TM-score 1.00
P12676 · AlphaFold monomer V2.0 prediction for cholesterol oxidase (P12676) · a predicted model of the same protein · 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 P12676
Elsewhere: RCSB PDB 1B8S · PDBe 1B8S · UniProt P12676

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