Research workbench

Tetrahydroprotoberberine N-methyltransferase in complex with (S)-cis- N-methylstylopine and S-adenosylhomocysteine

Analyse Tetrahydroprotoberberine N-methyltransferase in complex with (S)-cis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6P3O
Type: protein
Length: 341 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetrahydroprotoberberine N-methyltransferase
EC: 2.1.1.122
Ligands: SAH, SYT
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tetrahydroprotoberberine N-methyltransferase (EC 2.1.1.122)	protein	341	49% helix, 16% strand	—

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
SYT · (5s,12bs)-5-methyl-6,7,12B,13-tetrahydro-2H,4H,10H-[1, 3]dioxolo[4,5-g][1,3]dioxolo[7,8]isoquinolino[3,2-a]isoquinolin-5-ium · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 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	437	0.81	0.89	59	SAH, SYT
2	110	0.42	0.77	17	empty
3	68	0.36	0.77	15	empty

Compared structures

6P3O · Tetrahydroprotoberberine N-methyltransferase in complex with (S)-cis-N-methylstylopine… · 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
Elsewhere: RCSB PDB 6P3O · PDBe 6P3O

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