Research workbench
AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P48501)
Analyse AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P48501) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P48501
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Triosephosphate isomerase
- UniProt
- P48501
- Pockets
- 2 · best druggability 0.45
Structure
1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase | protein | 253 | 43% helix, 16% strand | P48501 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.45 | 0.77 | 21 | empty |
| 2 | 52 | 0.38 | 0.81 | 19 | empty |
Compared structures
- 6OOI · Crystal structure of triosephosphate isomerase from Schistosoma mansoni in complex with… · an experimental structure of the same protein · chain A against D, TM-score 0.98
- 6OOI · Crystal structure of triosephosphate isomerase from schistosoma mansoni in complex with… · an experimental structure of the same protein · chain A against D, TM-score 0.98
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 P48501
- Elsewhere: UniProt P48501 · AlphaFold DB P48501
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