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Wesselsbron virus methyltransferase in complex with sinefungin and 7MEGPPPA

Analyse Wesselsbron virus methyltransferase in complex with sinefungin and 7MEGPPPA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EMD
Type: protein
Length: 259 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyltransferase
EC: 2.1.1.57
UniProt: C8XPB0
Ligands: SFG, GTA, SO4
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methyltransferase (EC 2.1.1.57)	protein	259	38% helix, 17% strand	C8XPB0

Ligands and binding sites

SFG · Sinefungin · ligand · chains A
GTA · P1-7-methylguanosine-P3-adenosine-5',5'-triphosphate · ligand · chains A
SO4 · Sulfate ion · ion · 3 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	453	0.64	0.77	50	SFG, GTA, SO4

Compared structures

3EMD · Wesselsbron virus Methyltransferase in complex with Sinefungin and 7MeGpppA · 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 C8XPB0
Elsewhere: RCSB PDB 3EMD · PDBe 3EMD · UniProt C8XPB0

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