Research workbench
AlphaFold monomer V2.0 prediction for chloromuconate cycloisomerase (P05404)
Analyse AlphaFold monomer V2.0 prediction for chloromuconate cycloisomerase (P05404) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P05404
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- Chloromuconate cycloisomerase
- UniProt
- P05404
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chloromuconate cycloisomerase | protein | 370 | 42% helix, 23% strand | P05404 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.71 | 0.97 | 24 | empty |
| 2 | 129 | 0.41 | 0.75 | 18 | empty |
Compared structures
- 2CHR · A re-evaluation of the crystal structure of chloromuconate cycloisomerase · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 2CHR · A re-evaluation of the crystal structure of chloromuconate cycloisomerase · an experimental structure of the same protein · chain A against A, TM-score 0.99
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 P05404
- Elsewhere: UniProt P05404 · AlphaFold DB P05404
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