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MolNFT v1 · #116821 · protein

Crystal structure of ubig mutant in complex with sah

5DPM · Ubiquinone biosynthesis O-methyltransferase: “Crystal structure of ubig mutant in complex with sah”. X-ray diffraction, 1 ligand (SAH), 1 pocket (best druggability 0.74). MolNFT v1 #116821 on GenesisL1: 3D structure, binding sites…

PDB
5DPM
Type
protein
Length
206 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquinone biosynthesis O-methyltransferase
EC
2.1.1.222, 2.1.1.64
UniProt
A8A296
Ligands
SAH
Pockets
1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquinone biosynthesis O-methyltransferase (EC 2.1.1.222, 2.1.1.64)protein20640% helix, 28% strandA8A296

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13060.740.8646SAH

Compared structures

  • 5DPM · Crystal structure of UbiG mutant in complex with SAH · the same entry in another collection · chain A against A, TM-score 1.00
  • A8A296 · AlphaFold monomer V2.0 prediction for ubiquinone biosynthesis O-methyltransferase (A8A296) · a predicted model of the same protein · chain A against A, TM-score 0.97

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