Research workbench
AlphaFold monomer V2.0 prediction for putative metal-dependent hydrolase BAMEG_1894 (C3LH21)
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
- C3LH21
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9d37280c8D61e058C5085fA10417ECaD4341F28c
- Molecule
- Putative metal-dependent hydrolase BAMEG_1894
- UniProt
- C3LH21
- Pockets
- 1 · best druggability 0.53
Structure
1 distinct chain · 61% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative metal-dependent hydrolase BAMEG_1894 | protein | 173 | 61% helix, 6% strand | C3LH21 |
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 | 252 | 0.53 | 0.75 | 28 | 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 C3LH21
- Elsewhere: UniProt C3LH21 · AlphaFold DB C3LH21
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