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Structure of the crimean-congo haemorrhagic fever virus nucleocapsid protein

Analyse Structure of the crimean-congo haemorrhagic fever virus nucleocapsid protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AKL
Type: protein
Length: 946 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleocapsid
UniProt: Q70UR4
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nucleocapsid	protein	473	60% helix, 3% strand	Q70UR4

Ligands and binding sites

PGE · Triethylene glycol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 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	1100	0.82	0.83	83	empty
2	1052	0.82	0.83	71	empty
3	373	0.68	0.81	45	empty
4	56	0.32	0.77	13	empty
5	55	0.31	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 758 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4AKL · Structure of the Crimean-Congo Haemorrhagic Fever Virus Nucleocapsid Protein · 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 Q70UR4
Elsewhere: RCSB PDB 4AKL · PDBe 4AKL · UniProt Q70UR4

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