P-cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).

Ligands and binding sites

• FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
• HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, C, B, D
• CL · Chloride ion · ion · 2 copies · chains A, B
• TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 4 copies · chains A, B
• ACY · Acetic acid · additive · 4 copies · chains A, B

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

Pockets

17 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–B · 3619 Ų buried · 46 hydrogen bonds · protein-protein
• A–C · 1018 Ų buried · 10 hydrogen bonds · protein-protein
• B–D · 1013 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 cofactor (heme attachment, flavinylation).

Compared structures

• 1WVE · p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon… · the same entry in another collection · chain D against D, TM-score 1.00
• P09788 · AlphaFold monomer V2.0 prediction for 4-cresol dehydrogenase [hydroxylating] flavoprotein… · a predicted model of the same protein · chain A against A, TM-score 1.00
• P09787 · AlphaFold monomer V2.0 prediction for 4-cresol dehydrogenase [hydroxylating] cytochrome C… · a predicted model of the same protein · chain C against A, TM-score 0.99

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 P09788
• Every structure of UniProt P09787
• Elsewhere: RCSB PDB 1WVE · PDBe 1WVE · UniProt P09788 · UniProt P09787