Research workbench
AlphaFold monomer V2.0 prediction for probable metallo-hydrolase RV2300C (P9WLD7)
Analyse AlphaFold monomer V2.0 prediction for probable metallo-hydrolase RV2300C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P9WLD7
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBff4117c3aeAEEC3Deb08c0EF8C20B62bfBbb2cE
- Molecule
- Probable metallo-hydrolase RV2300C
- UniProt
- P9WLD7
- Pockets
- 4 · best druggability 0.57
Structure
1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable metallo-hydrolase RV2300C | protein | 310 | 30% helix, 22% strand | P9WLD7 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.57 | 0.84 | 25 | empty |
| 2 | 93 | 0.45 | 0.80 | 23 | empty |
| 3 | 91 | 0.37 | 0.75 | 17 | empty |
| 4 | 60 | 0.34 | 0.77 | 13 | empty |
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 P9WLD7
- Elsewhere: UniProt P9WLD7 · AlphaFold DB P9WLD7
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