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Investigation of the roles of catalytic residues in serotonin N- acetyltransferase

Analyse Investigation of the roles of catalytic residues in serotonin N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1L0C
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serotonin N-acetyltransferase
EC: 2.3.1.87
UniProt: Q29495
Ligands: COT
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serotonin N-acetyltransferase (EC 2.3.1.87)	protein	166	37% helix, 30% strand	Q29495

Ligands and binding sites

COT · Coa-S-acetyl tryptamine · ligand · 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	320	0.69	0.82	35	COT

Compared structures

1L0C · Investigation of the Roles of Catalytic Residues in Serotonin N-Acetyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
Q29495 · AlphaFold monomer V2.0 prediction for serotonin N-acetyltransferase (Q29495) · a predicted model of the same protein · 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 Q29495
Elsewhere: RCSB PDB 1L0C · PDBe 1L0C · UniProt Q29495

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