MolNFT v1 · #47286 · protein
Acetyltransferase domain of human HIV-1 tat interacting protein, 60KDA, isoform 3
2OU2 · Histone acetyltransferase htatip: “Acetyltransferase domain of human HIV-1 tat interacting protein, 60KDA, isoform 3”. X-ray diffraction, 2 ligands (ACO, ZN), 3 pockets (best druggability 0.70). MolNFT v1 #47286 on GenesisL1: 3D…
- PDB
- 2OU2
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase htatip
- EC
- 2.3.1.48
- UniProt
- Q92993
- Ligands
- ACO, ZN
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase htatip (EC 2.3.1.48) | protein | 246 | 33% helix, 24% strand | Q92993 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.70 | 0.84 | 38 | ACO |
| 2 | 85 | 0.37 | 0.76 | 16 | empty |
| 3 | 57 | 0.35 | 0.79 | 19 | empty |
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 2OU2 · Acetyltransferase domain of Human HIV-1 Tat interacting protein, 60kDa, isoform 3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q92993 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT5 (Q92993) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q92993
- Elsewhere: RCSB PDB 2OU2 · PDBe 2OU2 · UniProt Q92993
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