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Crystal structure of histone acetyltransferase HPA2 and related acetyltransferase (NP_600742.1) from corynebacterium glutamicum atcc 13032 at 1.90 a resolution

Analyse Crystal structure of histone acetyltransferase HPA2 and related… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QEC
Type: protein
Length: 181 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone acetyltransferase HPA2 and related acetyltransferases
UniProt: Q8NQB1
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase HPA2 and related acetyltransferases	protein	181	39% helix, 24% strand	Q8NQB1

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 9 copies · 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	599	0.68	0.77	63	EDO

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

2QEC · Crystal structure of histone acetyltransferase HPA2 and related acetyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q8NQB1
Elsewhere: RCSB PDB 2QEC · PDBe 2QEC · UniProt Q8NQB1

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