MolNFT v1 · #150967 · protein

Influenza a nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoem. conformation 1.

6H9G: “Influenza a nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex…”. Electron microscopy, 13 pockets (best druggability 0.50). MolNFT v1 #150967 on GenesisL1: 3D structure, binding sites and…

PDB: 6H9G
Type: protein
Length: 802 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein; Polypeptide loop
UniProt: Q1K9H2
Pockets: 13 · best druggability 0.50

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	Polypeptide loop	protein	19	0% helix, 16% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	159	0.50	0.78	30	empty
2	105	0.43	0.78	20	empty
3	115	0.42	0.76	19	empty
4	96	0.38	0.76	21	empty
5	62	0.37	0.79	13	empty

Interfaces

2 interfaces between chains.

A–B · 1593 Å² buried · 30 hydrogen bonds · protein-protein
C–D · 1591 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

6H9G · 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
Elsewhere: RCSB PDB 6H9G · PDBe 6H9G · UniProt Q1K9H2

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