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Crystal structure of tetrahymena GCN5 with bound coenzyme a and a 19-residue histone H3 peptide

Analyse Crystal structure of tetrahymena GCN5 with bound coenzyme a and a 19-residue… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PU9
Type: protein
Length: 178 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hat A1; Histone H3
UniProt: Q27198, P02303
Ligands: COA
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hat A1	protein	163	34% helix, 29% strand	Q27198
B	Histone H3	protein	15	0% helix, 0% strand	P02303

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	203	0.60	0.81	28	COA
2	118	0.40	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 918 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

1PU9 · Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3… · 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
Every structure of UniProt P02303
Elsewhere: RCSB PDB 1PU9 · PDBe 1PU9 · UniProt Q27198 · UniProt P02303

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