MolNFT v1 · #18866 · protein

Crystal structure of tetrahymena GCN5 with bound coenzyme a and a 19- residue histone H4 peptide

1Q2C · Histone acetyltransferase GCN5: “Crystal structure of tetrahymena GCN5 with bound coenzyme a and a 19- residue histone H4 peptide”. X-ray diffraction, 1 ligand (COA), 2 pockets (best druggability 0.62). MolNFT v1 #18866 on…

PDB: 1Q2C
Type: protein
Length: 170 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone acetyltransferase GCN5; Histone H4 peptide
EC: 2.3.1.-
UniProt: Q27198
Ligands: COA
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase GCN5 (EC 2.3.1.-)	protein	162	34% helix, 28% strand	Q27198
B	Histone H4 peptide	protein	8	0% helix, 0% strand	—

Ligands and binding sites

COA · Coenzyme A · ligand · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	202	0.62	0.82	27	COA
2	157	0.48	0.77	23	empty

Interfaces

1 interface between chains.

A–B · 515 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1Q2C · Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q27198
Elsewhere: RCSB PDB 1Q2C · PDBe 1Q2C · UniProt Q27198

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