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Cryo-EM structure of cchfv envelope protein gc in postfusion conformation

Analyse Cryo-EM structure of cchfv envelope protein gc in postfusion conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FGF
Type: protein
Length: 1,296 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoprotein C
UniProt: Q8JSZ3
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 5% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Glycoprotein C	protein	432	5% helix, 47% strand	Q8JSZ3

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1046	0.86	0.87	101	empty
2	510	0.83	0.89	53	empty
3	117	0.76	0.96	32	empty
4	115	0.76	0.96	29	empty
5	99	0.73	0.95	30	empty

Interfaces

3 interfaces between chains.

B–C · 2959 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 2956 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 2954 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 33 disulfide (disulfide).

Compared structures

7FGF · Cryo-EM structure of CCHFV envelope protein Gc in postfusion conformation · 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 Q8JSZ3
Elsewhere: RCSB PDB 7FGF · PDBe 7FGF · UniProt Q8JSZ3

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