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Crystal structure of arylalkylamine N-acetyltransferase 2 from aedes aegypti

Analyse Crystal structure of arylalkylamine N-acetyltransferase 2 from aedes aegypti in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FD5
Type: protein
Length: 216 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arylalkylamine N-acetyltransferase 2
EC: 2.3.1.87
UniProt: Q16KL9
Ligands: IOD
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arylalkylamine N-acetyltransferase 2 (EC 2.3.1.87)	protein	216	40% helix, 24% strand	Q16KL9

Ligands and binding sites

IOD · Iodide ion · ion · 8 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	961	0.81	0.82	74	IOD

Compared structures

4FD5 · Crystal structure of arylalkylamine N-Acetyltransferase 2 from Aedes aegypti · 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 Q16KL9
Elsewhere: RCSB PDB 4FD5 · PDBe 4FD5 · UniProt Q16KL9

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