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Crystal structure of arterivirus nonstructural protein 10 (helicase)

Analyse Crystal structure of arterivirus nonstructural protein 10 (helicase) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N0N
Type: protein
Length: 401 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Replicase polyprotein 1AB
EC: 3.4.22.-, 3.4.19.12, 3.4.21.-, 2.7.7.48, 3.6.4.12, 3.6.4.13
UniProt: P19811
Ligands: ZN, MG, SO4
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Replicase polyprotein 1AB (EC 3.4.22.-, 3.4.19.12, 3.4.21.-, 2.7.7.48, 3.6.4.12, 3.6.4.13)	protein	401	22% helix, 23% strand	P19811

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A
MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A

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

Pockets

2 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	1130	0.74	0.77	77	SO4, MG
2	120	0.58	0.85	28	empty

Compared structures

4N0N · Crystal structure of Arterivirus nonstructural protein 10 (helicase) · 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 P19811
Elsewhere: RCSB PDB 4N0N · PDBe 4N0N · UniProt P19811

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