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The crystal structure of inhibitor bound to jcv helicase

Analyse The crystal 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: 5J4V
Type: protein
Length: 358 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Large T antigen
EC: 3.6.4.-
UniProt: P03072
Ligands: 6JH, ZN, SO4
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Large T antigen (EC 3.6.4.-)	protein	358	59% helix, 8% strand	P03072

Ligands and binding sites

6JH · 2-(2-phenoxypyridin-3-yl)[1,3]thiazolo[5,4-c]pyridine · ligand · chains A
ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · 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	388	0.65	0.79	50	empty
2	93	0.52	0.83	13	empty
3	123	0.46	0.78	22	SO4, 6JH

Compared structures

5J4V · The crystal 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 5J4V · PDBe 5J4V · UniProt P03072

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