Reductive aminase from aspergillus terreus in complex with NADPH4, cyclohexanone and allyl amine

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 13% strand (DSSP).

Ligands and binding sites

• FVH · [[(2~{R},3~{S},4~{R},5~{R})-5-[(3~{R})-3-aminocarbonylpiperidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{R},4~{R}, 5~{R})-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate · ligand · 2 copies · chains A, B
• AYE · prop-2-en-1-amine · ligand · 2 copies · chains A, B
• CYH · Cyclohexanone · ligand · chains A, B

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.

Interfaces

1 interface between chains.

• A–B · 4274 Ų buried · 33 hydrogen bonds · protein-protein

Compared structures

• 6H7P · Reductive Aminase from Aspergillus terreus in complex with NADPH4, cyclohexa and allyl… · 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 Q0CCT3
• Elsewhere: RCSB PDB 6H7P · PDBe 6H7P · UniProt Q0CCT3