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Crystal structure of mete from streptococcus mutans

Analyse Crystal structure of mete 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
3L7R
Type
protein
Length
736 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
Ligands
ZN, SO4
Pockets
8 · 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)protein73646% helix, 15% strandQ8CWX6

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains A
  • SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111060.770.79106ZN
2740.730.9721empty
31520.630.8530empty
41640.610.8426empty
52500.600.7920empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3L7R · crystal structure of MetE 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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