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Crystal structure of the tick-borne encephalitis virus NS3 helicase in complex with amppnp

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

PDB: 7BM0
Type: protein
Length: 427 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NS3 helicase domain
EC: 3.6.4.13
UniProt: A0A2S1PWV0
Ligands: ANP, NA, MN
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NS3 helicase domain (EC 3.6.4.13)	protein	427	34% helix, 18% strand	A0A2S1PWV0

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
NA · Sodium ion · metal · 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

5 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	955	0.79	0.81	70	empty
2	200	0.54	0.79	35	ANP, MN
3	51	0.38	0.81	17	empty
4	54	0.38	0.80	19	empty
5	51	0.27	0.74	12	empty

Compared structures

7BM0 · Crystal structure of the tick-borne encephalitis virus NS3 helicase in complex with AMPPNP · 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 A0A2S1PWV0
Elsewhere: RCSB PDB 7BM0 · PDBe 7BM0 · UniProt A0A2S1PWV0

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