Research workbench
Crystal structure of human HBO1 in complex with BRPF2
Analyse Crystal structure of human HBO1 in complex with BRPF2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GK9
- Type
- protein
- Length
- 289 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT7; BRD1 protein
- EC
- 2.3.1.48
- UniProt
- O95251, Q86X06
- Ligands
- ACO, ZN
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT7 (EC 2.3.1.48) | protein | 265 | 35% helix, 27% strand | O95251 |
| B | BRD1 protein | protein | 24 | 0% helix, 58% strand | Q86X06 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.71 | 0.83 | 43 | ACO |
| 2 | 130 | 0.43 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 994 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 O95251
- Every structure of UniProt Q86X06
- Elsewhere: RCSB PDB 5GK9 · PDBe 5GK9 · UniProt O95251 · UniProt Q86X06
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