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Crystal structure of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase

Analyse Crystal structure of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3GMB
Type
protein
Length
738 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
UniProt
Q988D3
Ligands
FAD
Pockets
7 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenaseprotein36934% helix, 27% strandQ988D3

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19800.810.8396FAD
210930.810.8293FAD
31910.460.7526empty
42200.460.7430empty
51070.380.7520empty

Interfaces

1 interface between chains.

  • A–B · 721 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

  • 3GMB · Crystal Structure of 2-Methyl-3-hydroxypyridine-5-carboxylic acid Oxygenase · the same entry in another collection · chain A against A, TM-score 1.00

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