Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein MFLA_0145 (Q1H521)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein MFLA_0145… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1H521
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Nucleotide-binding protein MFLA_0145
- UniProt
- Q1H521
- Pockets
- 3 · best druggability 0.46
Structure
1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein MFLA_0145 | protein | 280 | 46% helix, 19% strand | Q1H521 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.46 | 0.76 | 25 | empty |
| 2 | 81 | 0.38 | 0.77 | 19 | empty |
| 3 | 53 | 0.38 | 0.81 | 14 | 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 Q1H521
- Elsewhere: UniProt Q1H521 · AlphaFold DB Q1H521
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