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Crystal structure of pa-PB1 complex form influenza virus RNA polymerase

Analyse Crystal structure of pa-PB1 complex form influenza virus RNA polymerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZNL
Type: protein
Length: 436 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase acidic protein; RNA-directed RNA polymerase catalytic subunit
EC: 2.7.7.48
UniProt: P03433, P03431
Pockets: 6 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase acidic protein	protein	421	41% helix, 19% strand	P03433
B	RNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48)	protein	15	40% helix, 13% strand	P03431

Pockets

6 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	323	0.64	0.80	32	empty
2	89	0.54	0.85	18	empty
3	141	0.45	0.76	19	empty
4	102	0.45	0.79	21	empty
5	112	0.38	0.74	24	empty

Interfaces

1 interface between chains.

A–B · 1136 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

2ZNL · Crystal structure of PA-PB1 complex form influenza virus RNA polymerase · 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
Every structure of UniProt P03431
Elsewhere: RCSB PDB 2ZNL · PDBe 2ZNL · UniProt P03433 · UniProt P03431

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