Research workbench

Structure of the zinc-binding domain of HCV NS5A

Analyse Structure of the zinc-binding domain of HCV NS5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZH1
Type: protein
Length: 326 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural polyprotein
UniProt: Q9WMX2
Ligands: ZN
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Non-structural polyprotein	protein	163	5% helix, 36% strand	Q9WMX2

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	921	0.76	0.79	76	empty
2	73	0.33	0.75	15	empty
3	52	0.31	0.76	13	empty
4	58	0.28	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 909 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1ZH1 · Structure of the zinc-binding domain of HCV NS5A · 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 Q9WMX2
Elsewhere: RCSB PDB 1ZH1 · PDBe 1ZH1 · UniProt Q9WMX2

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