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Influenza a virus nucleoprotein np at 3.2A resolution

Analyse Influenza a virus nucleoprotein np at 3.2A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IQH
Type: protein
Length: 1,288 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleocapsid protein
UniProt: Q1I2B5
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nucleocapsid protein	protein	426	46% helix, 9% strand	Q1I2B5
C	Nucleocapsid protein	protein	436	47% helix, 8% strand	Q1I2B5

Pockets

20 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	870	0.82	0.84	86	empty
2	193	0.66	0.85	37	empty
3	68	0.53	0.87	15	empty
4	110	0.47	0.80	23	empty
5	130	0.44	0.77	24	empty

Interfaces

3 interfaces between chains.

A–B · 2393 Å² buried · 39 hydrogen bonds · protein-protein
B–C · 2078 Å² buried · 46 hydrogen bonds · protein-protein
A–C · 2022 Å² buried · 44 hydrogen bonds · protein-protein

Compared structures

2IQH · Influenza A virus nucleoprotein NP at 3.2A resolution · 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 2IQH · PDBe 2IQH · UniProt Q1I2B5

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