Research workbench

Structure of zika virus NS5

Analyse Structure of zika virus NS5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TMH
Type: protein
Length: 1,760 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polyprotein
UniProt: A0A192GPS6
Ligands: SAH, ZN, SO4
Pockets: 20 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Polyprotein	protein	880	42% helix, 14% strand	A0A192GPS6

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 4 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1063	0.76	0.79	92	SO4
2	941	0.75	0.78	81	SO4
3	532	0.65	0.77	48	SAH
4	495	0.64	0.77	48	SAH
5	85	0.54	0.85	19	empty

Interfaces

1 interface between chains.

A–B · 883 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5TMH · Structure of Zika virus NS5 · the same entry in another collection · chain B against B, 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 A0A192GPS6
Elsewhere: RCSB PDB 5TMH · PDBe 5TMH · UniProt A0A192GPS6

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