Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized trans- sulfuration enzyme C23A1.14C (O42851)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized trans- sulfuration enzyme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O42851
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Uncharacterized trans-sulfuration enzyme C23A1.14C
- UniProt
- O42851
- Pockets
- 3 · best druggability 0.51
Structure
1 distinct chain · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized trans-sulfuration enzyme C23A1.14C | protein | 398 | 40% helix, 14% strand | O42851 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.51 | 0.82 | 25 | empty |
| 2 | 163 | 0.49 | 0.77 | 28 | empty |
| 3 | 77 | 0.37 | 0.77 | 21 | empty |
Compared structures
- 7YEO · Crystal Structure of cystathionine gamma-synthase-like protein C23A1.14c · an experimental structure of the same protein · chain A against B, TM-score 0.94
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 O42851
- Elsewhere: UniProt O42851 · AlphaFold DB O42851
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