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The N-terminal domain of pa endonuclease from the influenza H1N1 virus in complex with 3-hydroxy-4-oxo-4H-pyran-2-carboxylic acid

Analyse The N-terminal domain of pa endonuclease from the influenza H1N1 virus in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DCZ
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase acidic protein
EC: 3.1.-.-
UniProt: C3W5S0
Ligands: G5Y, MN
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase acidic protein (EC 3.1.-.-)	protein	180	51% helix, 13% strand	C3W5S0

Ligands and binding sites

G5Y · 3-hydroxy-4-oxo-4H-pyran-2-carboxylic acid · ligand · chains A
MN · Manganese (II) ion · metal · 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	520	0.66	0.77	45	G5Y, MN

Compared structures

6DCZ · The N-terminal domain of PA endonuclease from the influenza H1N1 virus in complex with… · 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 C3W5S0
Elsewhere: RCSB PDB 6DCZ · PDBe 6DCZ · UniProt C3W5S0

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