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Organization of the influenza virus replication machinery

Analyse Organization of the influenza virus replication machinery in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YMN
Type: protein
Length: 2,404 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein
UniProt: Q1I2B5
Pockets: 20 · best druggability 0.79

Structure

electron microscopy · 2 distinct chains · 48% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E, F	Nucleoprotein	protein	399	48% helix, 7% strand	Q1I2B5
C	Nucleoprotein	protein	409	49% helix, 7% strand	Q1I2B5

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	893	0.79	0.81	66	empty
2	979	0.78	0.80	74	empty
3	615	0.78	0.84	55	empty
4	743	0.78	0.82	53	empty
5	950	0.78	0.80	67	empty

Interfaces

8 interfaces between chains.

D–E · 505 Å² buried · 39 hydrogen bonds · protein-protein
E–F · 501 Å² buried · 38 hydrogen bonds · protein-protein
B–D · 317 Å² buried · 11 hydrogen bonds · protein-protein
A–E · 286 Å² buried · 0 hydrogen bonds · protein-protein
C–D · 145 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2YMN · Organization of the Influenza Virus Replication Machinery · 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 Q1I2B5
Elsewhere: RCSB PDB 2YMN · PDBe 2YMN · UniProt Q1I2B5

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