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Open crystal structure of cyclohexanone monooxygenase

Analyse Open crystal structure of cyclohexanone monooxygenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GWF
Type: protein
Length: 511 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclohexanone monooxygenase
EC: 1.14.13.22
UniProt: Q6RXW1
Ligands: FAD, NAP
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclohexanone monooxygenase (EC 1.14.13.22)	protein	511	37% helix, 22% strand	Q6RXW1

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1041	0.84	0.85	106	FAD, NAP
2	193	0.52	0.77	38	empty

Compared structures

3GWF · Open crystal structure of cyclohexa monooxygenase · 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 Q6RXW1
Elsewhere: RCSB PDB 3GWF · PDBe 3GWF · UniProt Q6RXW1

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