MolNFT v1 · #150143 · protein

Crystal structure of coclaurine N-methyltransferase (cnmt) bound to N- methylheliamine and sah

6GKY: “Crystal structure of coclaurine N-methyltransferase (cnmt) bound to N- methylheliamine and sah”. X-ray diffraction, 2 ligands (SAH, F2Z), 4 pockets (best druggability 0.87). MolNFT v1 #150143 on GenesisL1: 3D structure, binding…

PDB: 6GKY
Type: protein
Length: 702 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Coclaurine N-methyltransferase
EC: 2.1.1.115
UniProt: Q948P7
Ligands: SAH, F2Z
Pockets: 4 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Coclaurine N-methyltransferase (EC 2.1.1.115)	protein	351	46% helix, 16% strand	Q948P7

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
F2Z · 6,7-dimethoxy-2,4-dihydro-1~{H}-isoquinolin-3-one · ligand · 2 copies · chains A, B

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

Pockets

4 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	404	0.87	0.95	60	SAH, F2Z
2	633	0.85	0.89	80	SAH, F2Z
3	182	0.47	0.75	26	empty
4	53	0.29	0.75	16	empty

Compared structures

6GKY · Crystal structure of Coclaurine N-Methyltransferase (CNMT) bound to N-methylheliamine and… · 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 Q948P7
Elsewhere: RCSB PDB 6GKY · PDBe 6GKY · UniProt Q948P7

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