Research workbench

The human O-glcnacase C-terminal domain is a pseudo histone acetyltransferase

Analyse The human O-glcnacase C-terminal domain is a pseudo histone acetyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZJ0
Type: protein
Length: 202 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyltransferase
UniProt: Q2CEE2
Ligands: ACO, CL
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyltransferase	protein	202	40% helix, 22% strand	Q2CEE2

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · chains A
CL · Chloride ion · ion · 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	727	0.80	0.84	59	ACO, CL

Compared structures

3ZJ0 · The human O-GlcNAcase C-terminal domain is a pseudo histone acetyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
Q2CEE2 · AlphaFold monomer V2.0 prediction for putative acetyltransferase ogpat (Q2CEE2) · 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 Q2CEE2
Elsewhere: RCSB PDB 3ZJ0 · PDBe 3ZJ0 · UniProt Q2CEE2

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