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The crystal structure of wild type PA endonuclease (2009/H1N1/CALIFORNIA) in complex with compound SJ001023044

Analyse The crystal structure of wild type PA endonuclease (2009/H1N1/CALIFORNIA) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8DVO
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.33
Source: Influenza A virus
Molecule: Protein PA-X
UniProt: C6H0Y9
Ligands: U0I, QQ4, MN, SO4
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · resolution 2.33 · 1 distinct chain · 54% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein PA-X	protein	180	54% helix, 13% strand	C6H0Y9

Ligands and binding sites

U0I · 5-hydroxy-N-[2-(4-hydroxy-3-methoxyphenyl)ethyl]-6-oxo-2-{[2-(trifluoromethyl)phenyl]methyl}-1,6-dihydropyrimidine-4-carboxamide · ligand · chains A
QQ4 · Hexa Vinylpyrrolidone K15 · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	370	0.61	0.77	40	MN, U0I

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 C6H0Y9
Elsewhere: RCSB PDB 8DVO · PDBe 8DVO · UniProt C6H0Y9

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