MolNFT v1 · #163355 · protein

Structure of zika virus NS3 helicase in complex with ADP-MGF3(H2O)-

6S0J · Genome polyprotein: “Structure of zika virus NS3 helicase in complex with ADP-MGF3(H2O)-”. X-ray diffraction, 3 ligands (KQB, ADP, MG), 3 pockets (best druggability 0.82). MolNFT v1 #163355 on GenesisL1: 3D structure, binding sites…

PDB: 6S0J
Type: protein
Length: 433 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Genome polyprotein
UniProt: A0A160JCU6
Ligands: KQB, ADP, MG
Pockets: 3 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Genome polyprotein	protein	433	33% helix, 19% strand	A0A160JCU6

Ligands and binding sites

KQB · trifluoromagnesate monohydrate · ligand · chains A
ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 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	1084	0.82	0.83	83	empty
2	76	0.57	0.88	19	KQB, MG, ADP
3	54	0.26	0.73	18	empty

Compared structures

6S0J · Structure of Zika virus NS3 helicase in complex with ADP-MgF3(H2O)- · 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 A0A160JCU6
Elsewhere: RCSB PDB 6S0J · PDBe 6S0J · UniProt A0A160JCU6

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