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6-(3-METHOXYPHENYL)PYRIDINE-2,3-diol bound to influenza 2009 PH1N1 endonuclease

Analyse 6-(3-METHOXYPHENYL)PYRIDINE-2,3-diol bound to influenza 2009 PH1N1 endonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MK5
Type: protein
Length: 200 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase pa
UniProt: M9V5A4
Ligands: 28A, MN, SO4
Pockets: 1 · best druggability 0.62

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	M9V5A4

Ligands and binding sites

28A · 3-hydroxy-6-(3-methoxyphenyl)pyridin-2(5H)-one · ligand · chains A
MN · Manganese (II) ion · metal · 3 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

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	391	0.62	0.77	39	MN, EDO, 28A

Compared structures

4MK5 · 6-(3-methoxyphenyl)pyridine-2,3-diol bound to influenza 2009 pH1N1 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 M9V5A4
Elsewhere: RCSB PDB 4MK5 · PDBe 4MK5 · UniProt M9V5A4

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