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Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion

Analyse Tectonic conformational changes of a coronavirus spike glycoprotein promote… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6B3O
Type: protein
Length: 1,032 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spike glycoprotein
UniProt: P11224
Pockets: 12 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 44% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Spike glycoprotein	protein	344	44% helix, 22% strand	P11224

Pockets

12 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	88	0.78	0.99	16	empty
2	1193	0.75	0.77	87	empty
3	247	0.70	0.86	41	empty
4	364	0.60	0.77	47	empty
5	345	0.60	0.77	46	empty

Interfaces

3 interfaces between chains.

A–B · 6694 Å² buried · 67 hydrogen bonds · protein-protein
B–C · 6691 Å² buried · 67 hydrogen bonds · protein-protein
A–C · 6679 Å² buried · 67 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

6B3O · Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane… · 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 P11224
Elsewhere: RCSB PDB 6B3O · PDBe 6B3O · UniProt P11224

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