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Zika virus helicase in complex with ADP-ALF3

Analyse Zika virus helicase in complex with ADP-ALF3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Y6M
Type: protein
Length: 433 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Helicase domain from genome polyprotein
UniProt: A0A140GMI3
Ligands: ADP, AF3, MN
Pockets: 4 · best druggability 0.81

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Helicase domain from genome polyprotein	protein	433	34% helix, 19% strand	A0A140GMI3

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
AF3 · Aluminum fluoride · ligand · chains A
MN · Manganese (II) ion · metal · 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	1083	0.81	0.82	81	empty
2	170	0.57	0.81	31	MN, ADP, AF3
3	51	0.35	0.79	14	empty
4	72	0.32	0.75	20	empty

Compared structures

5Y6M · Zika virus helicase in complex with ADP-AlF3 · 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 A0A140GMI3
Elsewhere: RCSB PDB 5Y6M · PDBe 5Y6M · UniProt A0A140GMI3

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