Research workbench
Human GCN5 bound to propionyl-CoA
Analyse Human GCN5 bound to propionyl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H84
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT2A
- EC
- 2.3.1.48
- UniProt
- Q92830
- Ligands
- 1VU
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 164 | 34% helix, 29% strand | Q92830 |
Ligands and binding sites
- 1VU · propionyl Coenzyme A · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- IPA · Isopropyl alcohol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.57 | 0.79 | 35 | 1VU |
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 Q92830
- Elsewhere: RCSB PDB 5H84 · PDBe 5H84 · UniProt Q92830
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