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Hazara virus nucleocapsid protain

Analyse Hazara virus nucleocapsid protain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A97
Type: protein
Length: 1,906 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleocapsid protein
UniProt: M4PWE6
Pockets: 18 · best druggability 0.86

Structure

x-ray diffraction · 3 distinct chains · 60% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleocapsid protein	protein	473	60% helix, 3% strand	M4PWE6
B, D	Nucleocapsid protein	protein	477	60% helix, 3% strand	M4PWE6
C	Nucleocapsid protein	protein	479	60% helix, 3% strand	M4PWE6

Pockets

18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	862	0.86	0.88	74	empty
2	963	0.86	0.87	73	empty
3	1110	0.85	0.86	84	empty
4	1180	0.84	0.85	85	empty
5	476	0.76	0.85	53	empty

Interfaces

4 interfaces between chains.

C–D · 695 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 548 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 262 Å² buried · 1 hydrogen bond · protein-protein
A–D · 126 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5A97 · Hazara virus nucleocapsid protain · 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 M4PWE6
Elsewhere: RCSB PDB 5A97 · PDBe 5A97 · UniProt M4PWE6

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