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Cyclohexylamine oxidase from brevibacterium oxydans ih-35A

Analyse Cyclohexylamine oxidase from brevibacterium oxydans ih-35A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4I58
Type: protein
Length: 1,804 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclohexylamine oxidase
Ligands: FAD
Pockets: 15 · best druggability 0.87

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Cyclohexylamine oxidase	protein	451	37% helix, 22% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D

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

Pockets

15 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	493	0.87	0.94	63	FAD
2	489	0.87	0.94	62	FAD
3	503	0.87	0.93	62	FAD
4	527	0.86	0.92	64	FAD
5	719	0.78	0.82	79	empty

Interfaces

3 interfaces between chains.

C–D · 534 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 516 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 500 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4I58 · Cyclohexylamine Oxidase from Brevibacterium oxydans IH-35A · 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
Elsewhere: RCSB PDB 4I58 · PDBe 4I58

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