Research workbench

X-ray structure of cyclohexanone monooxygenase from acinetobacter calcoaceticus

Analyse X-ray structure of cyclohexanone monooxygenase from acinetobacter calcoaceticus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6A37
Type: protein
Length: 510 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative flavin-binding monooxygenase
UniProt: A0A0A8XFY0
Ligands: FAD
Pockets: 5 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative flavin-binding monooxygenase	protein	510	36% helix, 21% strand	A0A0A8XFY0

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

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	976	0.81	0.83	90	FAD
2	192	0.57	0.80	29	empty
3	69	0.51	0.85	20	empty
4	87	0.38	0.76	19	empty
5	113	0.36	0.74	24	empty

Compared structures

6A37 · X-ray structure of cyclohexa monooxygenase from Acinetobacter calcoaceticus · 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 A0A0A8XFY0
Elsewhere: RCSB PDB 6A37 · PDBe 6A37 · UniProt A0A0A8XFY0

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