Research workbench

Human GCN5 bound to butyryl-CoA

Analyse Human GCN5 bound to butyryl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5H86
Type: protein
Length: 167 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: BCO
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase KAT2A (EC 2.3.1.48)	protein	167	34% helix, 28% strand	Q92830

Ligands and binding sites

BCO · Butyryl Coenzyme A · ligand · chains A
EDO · 1,2-ethanediol · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	288	0.59	0.78	31	BCO

Compared structures

5H86 · Human Gcn5 bound to butyryl-CoA · the same entry in another collection · chain A against A, TM-score 1.00
Q92830 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT2A (Q92830) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 5H86 · PDBe 5H86 · UniProt Q92830

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