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Crystal structure of T-protein of the glycine cleavage system

Analyse Crystal structure of T-protein of the glycine cleavage system in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WOR
Type
protein
Length
362 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aminomethyltransferase
EC
2.1.2.10
UniProt
Q9WY54
Ligands
RED
Pockets
2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAminomethyltransferase (EC 2.1.2.10)protein36224% helix, 36% strandQ9WY54

Ligands and binding sites

  • RED · Dihydrolipoic acid · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15640.720.8071RED
21080.380.7514empty

Compared structures

  • 1WOR · Crystal Structure of T-protein of the Glycine Cleavage System · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WY54 · AlphaFold monomer V2.0 prediction for aminomethyltransferase (Q9WY54) · a predicted model of the same protein · chain A against A, TM-score 1.00

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