MolNFT v1 · #153120 · protein

Lepi-sah complex structure

6J46 · O-methyltransferase lepi: “Lepi-sah complex structure”. X-ray diffraction, 1 ligand (SAH), 7 pockets (best druggability 0.86). MolNFT v1 #153120 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6J46
Type: protein
Length: 774 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: O-methyltransferase lepi
EC: 2.1.1.-
UniProt: B8NJH3
Ligands: SAH
Pockets: 7 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	O-methyltransferase lepi (EC 2.1.1.-)	protein	387	53% helix, 12% strand	B8NJH3

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1152	0.86	0.87	95	SAH
2	1199	0.86	0.87	97	SAH
3	217	0.56	0.79	26	empty
4	193	0.53	0.78	24	empty
5	99	0.46	0.81	18	empty

Interfaces

1 interface between chains.

A–B · 5143 Å² buried · 46 hydrogen bonds · protein-protein

Compared structures

6J46 · LepI-SAH complex structure · the same entry in another collection · chain B against B, TM-score 1.00
B8NJH3 · AlphaFold monomer V2.0 prediction for O-methyltransferase lepi (B8NJH3) · a predicted model of the same protein · chain B 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 B8NJH3
Elsewhere: RCSB PDB 6J46 · PDBe 6J46 · UniProt B8NJH3

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