Research workbench
AlphaFold monomer V2.0 prediction for PDZ and lim domain protein zasp (A1ZA47)
Analyse AlphaFold monomer V2.0 prediction for PDZ and lim domain protein zasp (A1ZA47) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1ZA47
- Type
- protein
- Length
- 2,194 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x754211C7Fae7D5307c457b846C626ab75786652A
- Molecule
- PDZ and lim domain protein zasp
- UniProt
- A1ZA47
- Pockets
- 10 · best druggability 0.53
Structure
1 distinct chain · 10% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PDZ and lim domain protein zasp | protein | 2194 | 10% helix, 5% strand | A1ZA47 |
Pockets
10 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 327 | 0.53 | 0.74 | 40 | empty |
| 2 | 221 | 0.48 | 0.74 | 19 | empty |
| 3 | 148 | 0.42 | 0.74 | 16 | empty |
| 4 | 138 | 0.42 | 0.75 | 24 | empty |
| 5 | 72 | 0.34 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 1 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 A1ZA47
- Elsewhere: UniProt A1ZA47 · AlphaFold DB A1ZA47
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