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Crystal structure of dengue methyltransferase in complex with gpppg and S-adenosyl-L-homocysteine

Analyse Crystal structure of dengue methyltransferase in complex with gpppg and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P3Q
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Type II methyltransferase
EC: 2.7.7.48
UniProt: Q9WLZ8
Ligands: GP3, SAH, SO4
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Type II methyltransferase (EC 2.7.7.48)	protein	258	36% helix, 16% strand	Q9WLZ8

Ligands and binding sites

GP3 · Diguanosine-5'-triphosphate · ligand · chains A
SAH · S-adenosyl-L-homocysteine · ligand · chains A
SO4 · Sulfate ion · ion · 6 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	528	0.65	0.77	52	SO4, GP3, SAH

Compared structures

2P3Q · Crystal Structure of Dengue Methyltransferase in Complex with GpppG 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 Q9WLZ8
Elsewhere: RCSB PDB 2P3Q · PDBe 2P3Q · UniProt Q9WLZ8

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