Research workbench
Crystal structure of human HBO1-BRPF2 in complex with succinyl-coenzyme A
Analyse Crystal structure of human HBO1-BRPF2 in complex with succinyl-coenzyme A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D0S
- Type
- protein
- Length
- 302 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Homo sapiens
- Molecule
- Histone acetyltransferase KAT7; BRD1 protein
- EC
- 2.3.1.48
- UniProt
- O95251, Q86X06
- Ligands
- SCA, ZN
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT7 (EC 2.3.1.48) | protein | 274 | 38% helix, 26% strand | O95251 |
| B | BRD1 protein | protein | 28 | 0% helix, 36% strand | Q86X06 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.69 | 0.83 | 35 | SCA |
| 2 | 75 | 0.50 | 0.84 | 20 | empty |
| 3 | 63 | 0.45 | 0.83 | 19 | empty |
| 4 | 143 | 0.42 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 927 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 7D0S · Crystal structure of human HBO1-BRPF2 in complex with succinyl- coenzyme a · the same entry in another collection · chain A against A, TM-score 1.00
- O95251 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT7 (O95251) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 7D0S · PDBe 7D0S · UniProt O95251 · UniProt Q86X06
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