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The structure of triosephosphate isomerase from escherichia COLI determined at 2.6 ångström resolution

Analyse The structure of triosephosphate isomerase from escherichia COLI determined at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TRE
Type
protein
Length
508 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Triosephosphate isomerase
EC
5.3.1.1
UniProt
P0A858
Pockets
4 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATriosephosphate isomerase (EC 5.3.1.1)protein25549% helix, 15% strandP0A858
BTriosephosphate isomerase (EC 5.3.1.1)protein25347% helix, 15% strandP0A858

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13070.690.8446empty
21410.450.7631empty
31030.440.7821empty
4510.360.8014empty

Interfaces

1 interface between chains.

  • A–B · 1710 Ų buried · 40 hydrogen bonds · protein-protein

Compared structures

  • 1TRE · The structure of triosephosphate isomerase from escherichia COLI determined at 2.6… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A858 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P0A858) · a predicted model of the same protein · chain B against A, TM-score 0.98

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