MolNFT v1 · #420006 · protein
AlphaFold monomer V2.0 prediction for histone deacetylase complex subunit SAP18 (O55128)
O55128: “AlphaFold monomer V2.0 prediction for histone deacetylase complex subunit SAP18 (O55128)”. 1 pocket (best druggability 0.26). MolNFT v1 #420006 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- O55128
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4B52824A4D328C948b0b9091b60434807b691D00
- Molecule
- Histone deacetylase complex subunit SAP18
- UniProt
- O55128
- Pockets
- 1 · best druggability 0.26
Structure
1 distinct chain · 18% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone deacetylase complex subunit SAP18 | protein | 153 | 18% helix, 28% strand | O55128 |
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 | 51 | 0.26 | 0.73 | 11 | empty |
Compared structures
- 4A6Q · Crystal structure of mouse SAP18 residues 6-143 · an experimental structure of the same protein · chain A against A, TM-score 0.90
- 4A6Q · Crystal structure of mouse SAP18 residues 6-143 · an experimental structure of the same protein · chain A against A, TM-score 0.90
- 4A90 · Crystal structure of mouse SAP18 residues 1-143 · an experimental structure of the same protein · chain A against B, TM-score 0.81
- 4A90 · Crystal structure of mouse SAP18 residues 1-143 · an experimental structure of the same protein · chain A against B, TM-score 0.81
- 4A8X · Structure of the core asap complex · an experimental structure of the same protein · chain A against C, TM-score 0.79
- 4A8X · Structure of the core ASAP complex · an experimental structure of the same protein · chain A against C, TM-score 0.79
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 O55128
- Elsewhere: UniProt O55128 · AlphaFold DB O55128
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