Tetrameric form of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (mhpco)

Structure

x-ray diffraction · 3 distinct chains · 35% helix, 28% strand (DSSP).

Ligands and binding sites

• FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
• SO4 · Sulfate ion · ion · 12 copies · chains A, B, C, D
• EDO · 1,2-ethanediol · additive · 51 copies · chains A, C, B, D
• PEG · Di(hydroxyethyl)ether · additive · 22 copies · chains A, B, C, D
• BME · Beta-mercaptoethanol · additive · 4 copies · chains A, B, C, D
• PG4 · Tetraethylene glycol · additive · 3 copies · chains A, B, C, D
• PGE · Triethylene glycol · additive · 2 copies · chains A, B, D

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

Pockets

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

Interfaces

6 interfaces between chains.

• C–D · 902 Ų buried · 13 hydrogen bonds · protein-protein
• A–B · 888 Ų buried · 13 hydrogen bonds · protein-protein
• A–C · 323 Ų buried · 1 hydrogen bond · protein-protein
• B–D · 323 Ų buried · 1 hydrogen bond · protein-protein
• B–C · 63 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 covalent (additive adduct).

Compared structures

• 4H2P · Tetrameric form of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) · 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 Q988D3
• Elsewhere: RCSB PDB 4H2P · PDBe 4H2P · UniProt Q988D3