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The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase

Analyse The crystal structure of the "open" and the "closed" conformation of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TIM
Type
protein
Length
498 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Triosephosphate isomerase
EC
5.3.1.1
UniProt
P04789
Pockets
3 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BTriosephosphate isomerase (EC 5.3.1.1)protein24945% helix, 17% strandP04789

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11640.440.7428empty
21380.440.7635empty
3560.270.7418empty

Interfaces

1 interface between chains.

  • A–B · 1580 Ų buried · 31 hydrogen bonds · protein-protein

Compared structures

  • 3TIM · The crystal structure of the "open" and the "closed" conformation of the flexible loop of… · 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 1.00
  • 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 1.00

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