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Influenza a nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoem. conformation 3.

Analyse Influenza a nucleoprotein docked into 3D helical structure of the wild type… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6I7B
Type: protein
Length: 802 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein
UniProt: Q1K9H2, P15682
Pockets: 14 · best druggability 0.45

Structure

electron microscopy · 2 distinct chains · 45% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Nucleoprotein	protein	382	47% helix, 8% strand	Q1K9H2
B, D	Nucleoprotein	protein	19	0% helix, 16% strand	P15682

Pockets

14 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	115	0.45	0.78	20	empty
2	98	0.44	0.79	22	empty
3	114	0.44	0.77	22	empty
4	83	0.41	0.78	19	empty
5	144	0.41	0.74	38	empty

Interfaces

2 interfaces between chains.

A–B · 1591 Å² buried · 30 hydrogen bonds · protein-protein
C–D · 1590 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

6I7B · Influenza A nucleoprotein docked into 3D helical structure of the wild type… · 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 Q1K9H2
Every structure of UniProt P15682
Elsewhere: RCSB PDB 6I7B · PDBe 6I7B · UniProt Q1K9H2 · UniProt P15682

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