Research workbench
AlphaFold monomer V2.0 prediction for zinc finger protein 512 (Q96ME7)
Analyse AlphaFold monomer V2.0 prediction for zinc finger protein 512 (Q96ME7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96ME7
- Type
- protein
- Length
- 567 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x061709E5c590470B2a4D9a39A6B73b43637aa6A5
- Molecule
- Zinc finger protein 512
- UniProt
- Q96ME7
- Pockets
- 1 · best druggability 0.29
Structure
1 distinct chain · 30% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger protein 512 | protein | 567 | 30% helix, 5% strand | Q96ME7 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.29 | 0.72 | 16 | empty |
Compared structures
- 2CTD · Solution structure of two zf-C2H2 domains from human Zinc finger protein 512 · an experimental structure of the same protein · chain A against A, TM-score 0.09
- 2CTD · Solution structure of two zf-C2H2 domains from human zinc finger protein 512 · an experimental structure of the same protein · chain A against A, TM-score 0.09
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 Q96ME7
- Elsewhere: UniProt Q96ME7 · AlphaFold DB Q96ME7
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