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Crystal structure of methyltransferase from streptococcus mutans

Analyse Crystal structure of methyltransferase from streptococcus mutans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NQ5
Type
protein
Length
706 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
EC
2.1.1.14
UniProt
Q8CWX6
Pockets
9 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14)protein70646% helix, 15% strandQ8CWX6

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16320.770.8260empty
2670.730.9821empty
31260.680.9021empty
44870.650.7742empty
52300.570.7921empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 2NQ5 · Crystal structure of methyltransferase from Streptococcus mutans · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8CWX6 · AlphaFold monomer V2.0 prediction for 5-methyltetrahydropteroyltriglutamate--homocysteine… · a predicted model of the same protein · chain A against A, TM-score 0.98

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