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Apo form of influenza strain H1N1 polymerase acidic subunit N-terminal region crystallized with polyethylene glycol 8000

Analyse Apo form of influenza strain H1N1 polymerase acidic subunit N-terminal region… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JHV
Type: protein
Length: 362 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase acidic protein
UniProt: P03433
Ligands: MN
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Polymerase acidic protein	protein	181	52% helix, 13% strand	P03433

Ligands and binding sites

MN · Manganese (II) ion · metal · 4 copies · chains A, B

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	585	0.71	0.79	52	MN
2	531	0.67	0.77	46	MN

Interfaces

1 interface between chains.

A–B · 627 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5JHV · Apo form of influenza strain H1N1 polymerase acidic subunit N-terminal region… · 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 P03433
Elsewhere: RCSB PDB 5JHV · PDBe 5JHV · UniProt P03433

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