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AlphaFold monomer V2.0 prediction for protein kinase C-binding protein NELL2 (A2VCU8)
Analyse AlphaFold monomer V2.0 prediction for protein kinase C-binding protein NELL2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2VCU8
- Type
- protein
- Length
- 814 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Protein kinase C-binding protein NELL2
- UniProt
- A2VCU8
- Pockets
- 8 · best druggability 0.52
Structure
1 distinct chain · 11% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase C-binding protein NELL2 | protein | 814 | 11% helix, 39% strand | A2VCU8 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.52 | 0.76 | 24 | empty |
| 2 | 190 | 0.45 | 0.74 | 21 | empty |
| 3 | 118 | 0.42 | 0.76 | 17 | empty |
| 4 | 111 | 0.39 | 0.75 | 17 | empty |
| 5 | 124 | 0.38 | 0.73 | 20 | empty |
Modifications
Observed in the structure: 42 disulfide (disulfide).
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 A2VCU8
- Elsewhere: UniProt A2VCU8 · AlphaFold DB A2VCU8
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