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7-(4-fluorophenyl)-3-hydroxyquinolin-2(1H)-one bound to influenza 2009 H1N1 endonuclease

Analyse 7-(4-fluorophenyl)-3-hydroxyquinolin-2(1H)-one bound to influenza 2009 H1N1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KIL
Type: protein
Length: 200 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase pa
UniProt: F0TRT1
Ligands: 1R5, MN, SO4
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase pa	protein	200	48% helix, 16% strand	F0TRT1

Ligands and binding sites

1R5 · 7-(4-fluorophenyl)-3-hydroxyquinolin-2(1H)-one · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	316	0.57	0.76	36	MN, EDO, 1R5
2	72	0.47	0.82	19	empty

Compared structures

4KIL · 7-(4-fluorophenyl)-3-hydroxyquinolin-2(1H)-one bound to influenza 2009 H1N1 endonuclease · 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 F0TRT1
Elsewhere: RCSB PDB 4KIL · PDBe 4KIL · UniProt F0TRT1

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