Research workbench
AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase, glycosomal (P13377)
Analyse AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase, glycosomal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P13377
- Type
- protein
- Length
- 607 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- UniProt
- P13377
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 607 | — | P13377 |
Compared structures
- 2O2D · Crystal structure of phosphoglucose isomerase from trypanosoma brucei complexed with… · an experimental structure of the same protein · chain A against B, TM-score 0.93
- 2O2D · Crystal structure of phosphoglucose isomerase from Trypanosoma brucei complexed with… · an experimental structure of the same protein · chain A against B, TM-score 0.93
- 2O2C · Crystal structure of phosphoglucose isomerase from T. brucei containing… · an experimental structure of the same protein · chain A against B, TM-score 0.93
- 2O2C · Crystal structure of phosphoglucose isomerase from T. brucei containing… · an experimental structure of the same protein · chain A against B, TM-score 0.93
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 P13377
- Elsewhere: UniProt P13377 · AlphaFold DB P13377
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