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Pandda analysis group deposition -- crystal structure of zika virus NS3 helicase in complex with Z235341991

Analyse Pandda analysis group deposition -- crystal structure of zika virus NS3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5RHG
Type: protein
Length: 435 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NS3 helicase
EC: 3.4.21.91, 3.6.1.15, 3.6.4.13
UniProt: Q32ZE1
Ligands: NY7, PO4
Pockets: 3 · best druggability 0.79

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NS3 helicase (EC 3.4.21.91, 3.6.1.15, 3.6.4.13)	protein	435	34% helix, 19% strand	Q32ZE1

Ligands and binding sites

NY7 · N-(2-methoxy-5-methylphenyl)glycinamide · ligand · 2 copies · chains A
PO4 · Phosphate ion · ion · 3 copies · chains A
EDO · 1,2-ethanediol · 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	989	0.79	0.81	71	EDO, PO4, NY7
2	207	0.59	0.81	38	PO4
3	103	0.38	0.75	23	empty

Compared structures

5RHG · PanDDA analysis group deposition -- Crystal Structure of Zika virus NS3 Helicase in… · the same entry in another collection · chain A against A, TM-score 1.00

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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 5RHG · PDBe 5RHG · UniProt Q32ZE1

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