Research workbench
AlphaFold monomer V2.0 prediction for putative metal-dependent hydrolase BCAH820_2714 (B7JQU1)
Analyse AlphaFold monomer V2.0 prediction for putative metal-dependent hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7JQU1
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC8051e607417A2890274BC226Eb475379945EA5C
- Molecule
- Putative metal-dependent hydrolase BCAH820_2714
- UniProt
- B7JQU1
- Pockets
- 1 · best druggability 0.52
Structure
1 distinct chain · 62% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative metal-dependent hydrolase BCAH820_2714 | protein | 173 | 62% helix, 6% strand | B7JQU1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.52 | 0.75 | 27 | 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 B7JQU1
- Elsewhere: UniProt B7JQU1 · AlphaFold DB B7JQU1
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