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Structure of affimer-np bound to crimean-congo haemorrhagic fever virus nucleocapsid protein

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

PDB: 6Z0O
Type: protein
Length: 1,126 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleocapsid; Affimer-np
UniProt: Q70UR4
Pockets: 11 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nucleocapsid	protein	473	59% helix, 3% strand	Q70UR4
E, F	Affimer-np	protein	90	20% helix, 60% strand	—

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	976	0.85	0.86	86	empty
2	1145	0.83	0.84	82	empty
3	117	0.77	0.95	27	empty
4	351	0.64	0.79	31	empty
5	237	0.53	0.77	32	empty

Interfaces

3 interfaces between chains.

A–E · 707 Å² buried · 9 hydrogen bonds · protein-protein
B–F · 633 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 378 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6Z0O · Structure of Affimer-NP bound to Crimean-Congo Haemorrhagic Fever Virus Nucleocapsid… · the same entry in another collection · chain A against A, TM-score 1.00

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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 6Z0O · PDBe 6Z0O · UniProt Q70UR4

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