Research workbench
The monomerization of triosephosphate isomerase from trypanosoma cruzi
Analyse The monomerization of triosephosphate isomerase from trypanosoma cruzi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V5B
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P52270
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 237 | 49% helix, 17% strand | P52270 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.44 | 0.74 | 27 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 2V5B · The monomerization of Triosephosphate Isomerase from Trypanosoma cruzi · the same entry in another collection · chain A against A, TM-score 1.00
- P52270 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, glycosomal (P52270) · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P52270
- Elsewhere: RCSB PDB 2V5B · PDBe 2V5B · UniProt P52270
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