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Crystallographic structure of GM23 an example of catalytic migration from tim to thiamin phosphate synthase.

Analyse Crystallographic structure of GM23 an example of catalytic migration from tim… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Y6Z
Type
protein
Length
256 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Triose-phosphate isomerase
EC
5.3.1.1
UniProt
P04789
Ligands
TPS, POP
Pockets
2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATriose-phosphate isomerase (EC 5.3.1.1)protein25645% helix, 16% strandP04789

Ligands and binding sites

  • TPS · Thiamin phosphate · ligand · chains A
  • POP · Pyrophosphate 2- · 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
11840.540.7929TPS
2950.390.7618empty

Compared structures

  • 2Y6Z · Crystallographic structure of GM23 an example of Catalytic migration from TIM to thiamin… · the same entry in another collection · chain A against A, TM-score 1.00
  • 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.90

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