MolNFT v1 · #2170 · protein

Histone acetyltransferase HAT1 from saccharomyces cerevisiae in complex with acetyl coenzyme a

1BOB: “Histone acetyltransferase HAT1 from saccharomyces cerevisiae in complex with acetyl coenzyme a”. X-ray diffraction, 2 ligands (ACO, CA), 1 pocket (best druggability 0.60). MolNFT v1 #2170 on GenesisL1: 3D structure, binding sites…

PDB: 1BOB
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone acetyltransferase
EC: 2.3.1.48
UniProt: Q12341
Ligands: ACO, CA
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase (EC 2.3.1.48)	protein	306	36% helix, 28% strand	Q12341

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · chains A
CA · Calcium ion · metal · 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	256	0.60	0.79	32	ACO

Compared structures

1BOB · Histone acetyltransferase HAT1 from saccharomyces cerevisiae in complex with acetyl… · the same entry in another collection · chain A against A, TM-score 1.00
Q12341 · AlphaFold monomer V2.0 prediction for histone acetyltransferase type B catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q12341
Elsewhere: RCSB PDB 1BOB · PDBe 1BOB · UniProt Q12341

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