MolNFT v1 · #142738 · protein

Crystal structure of the zika virus NS3 helicase (apo form)

6ADW · Serine protease NS3: “Crystal structure of the zika virus NS3 helicase (apo form)”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.81). MolNFT v1 #142738 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6ADW
Type: protein
Length: 434 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine protease NS3
EC: 3.4.21.91, 3.6.1.15, 3.6.4.13
UniProt: Q32ZE1
Ligands: SO4
Pockets: 3 · best druggability 0.81

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease NS3 (EC 3.4.21.91, 3.6.1.15, 3.6.4.13)	protein	434	33% helix, 19% strand	Q32ZE1

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine 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	996	0.81	0.82	94	SO4
2	85	0.66	0.92	24	EPE
3	51	0.25	0.73	11	empty

Compared structures

6ADW · Crystal structure of the Zika virus NS3 helicase (apo form) · 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 Q32ZE1
Elsewhere: RCSB PDB 6ADW · PDBe 6ADW · UniProt Q32ZE1

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