Research workbench

The X-ray structure of Inhibitor Bound to JCV Helicase

Analyse The X-ray structure of Inhibitor Bound to JCV Helicase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J47
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.99
Source: JC polyomavirus
Molecule: Large T antigen
EC: 3.6.4.-
UniProt: P03072
Ligands: 6JJ, ZN
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · resolution 1.99 · 1 distinct chain · 58% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Large T antigen (EC 3.6.4.-)	protein	360	58% helix, 8% strand	P03072

Ligands and binding sites

6JJ · 6-(2-phenoxyphenyl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole · ligand · chains A
ZN · Zinc ion · metal · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	399	0.63	0.78	48	empty
2	96	0.52	0.82	13	empty
3	94	0.43	0.78	17	6JJ

Compared structures

5J47 · The X-ray structure of inhibitor bound to jcv helicase · 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 P03072
Elsewhere: RCSB PDB 5J47 · PDBe 5J47 · UniProt P03072

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