Research workbench
AlphaFold monomer V2.0 prediction for enolase (P0A6P9)
Analyse AlphaFold monomer V2.0 prediction for enolase (P0A6P9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A6P9
- Type
- protein
- Length
- 432 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x29d49a7361954F998e834274B160AAE7B6751739
- UniProt
- P0A6P9
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 432 | — | P0A6P9 |
Compared structures
- 5OHG · enolase in complex with RNase E · an experimental structure of the same protein · chain A against B, TM-score 1.00
- 5OHG · Enolase in complex with RNase E · an experimental structure of the same protein · chain A against B, TM-score 1.00
- 3H8A · Crystal structure of E. coli enolase bound to its cognate RNase E recognition domain · an experimental structure of the same protein · chain A against D, TM-score 0.99
- 3H8A · Crystal structure of E. COLI enolase bound to its cognate RNase E recognition domain · an experimental structure of the same protein · chain A against D, TM-score 0.99
- 2FYM · Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase… · an experimental structure of the same protein · chain A against F, TM-score 0.98
- 2FYM · Crystal structure of E. COLI enolase complexed with the minimal binding segment of RNase… · an experimental structure of the same protein · chain A against F, 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 P0A6P9
- Elsewhere: UniProt P0A6P9 · AlphaFold DB P0A6P9
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