Research workbench

Structural and mechanistic analysis of drosophila melanogaster polyamine N acetyltransferase, an enzyme that catalyzes the formation of N acetylagmatine

Analyse Structural and mechanistic analysis of drosophila melanogaster polyamine N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5K9N
Type: protein
Length: 419 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polyamine N acetyltransferase
EC: 2.3.1.-
UniProt: Q9W469
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polyamine N acetyltransferase (EC 2.3.1.-)	protein	210	42% helix, 25% strand	Q9W469
B	Polyamine N acetyltransferase (EC 2.3.1.-)	protein	209	44% helix, 25% strand	Q9W469

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	688	0.81	0.85	83	empty
2	532	0.78	0.85	81	empty

Interfaces

1 interface between chains.

A–B · 983 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

5K9N · Structural and Mechanistic Analysis of Drosophila melanogaster Polyamine N… · 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 Q9W469
Elsewhere: RCSB PDB 5K9N · PDBe 5K9N · UniProt Q9W469

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.