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Crystal structure of the zika virus NS3 helicase

Analyse Crystal structure of the zika virus NS3 helicase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VI7
Type: protein
Length: 435 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Helicase
EC: 3.6.4.13
UniProt: Q32ZE1
Ligands: SO4
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Helicase (EC 3.6.4.13)	protein	435	34% helix, 19% strand	Q32ZE1

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	1165	0.82	0.83	100	SO4
2	223	0.60	0.81	43	SO4
3	89	0.35	0.75	21	empty
4	50	0.24	0.72	14	empty

Compared structures

5VI7 · Crystal structure of the Zika virus NS3 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 Q32ZE1
Elsewhere: RCSB PDB 5VI7 · PDBe 5VI7 · UniProt Q32ZE1

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