Eugenol oxidase from rhodococcus jostii: mutant S81H, A423M, H434Y, S394V, I445D, S518P

Structure

x-ray diffraction · resolution 2.8 · 5 distinct chains · 39% helix, 19% strand (DSSP).

Ligands and binding sites

• FAD · Flavin-adenine dinucleotide · ligand · 6 copies · chains A, C, D, E, G, H
• EOL · 2-methoxy-4-(prop-2-en-1-yl)phenol · ligand · 5 copies · chains A, C, D, E, G
• I7I · [[(2~{S},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{S})-5-[5-[(1~{R})-1-(3-methoxy-4-oxidanyl-phenyl)propyl]-7,8-dimethyl-2,4-bis(oxidanylidene)-1~{H}-benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate · ligand · 2 copies · chains B, F
• HEZ · Hexane-1,6-diol · additive · 4 copies · chains A, D, B, C
• GOL · Glycerol · additive · 2 copies · chains A, C

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

10 interfaces between chains.

• B–C · 3572 Ų buried · 39 hydrogen bonds · protein-protein
• A–D · 3552 Ų buried · 39 hydrogen bonds · protein-protein
• E–G · 3531 Ų buried · 37 hydrogen bonds · protein-protein
• F–H · 3523 Ų buried · 33 hydrogen bonds · protein-protein
• A–F · 722 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 cofactor, 2 covalent (flavinylation, covalent ligand).

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 Q0SBK1
• Elsewhere: RCSB PDB 7YWU · PDBe 7YWU · UniProt Q0SBK1