Research workbench

Ccov-hupn-2018 S in the swung out conformation (local refinement of domain 0)

Analyse Ccov-hupn-2018 S in the swung out conformation (local refinement of domain 0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7USB
Type: protein
Length: 213 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spike glycoprotein
UniProt: A0A8E6CMP0
Ligands: NAG
Pockets: 1 · best druggability 0.62

Structure

electron microscopy · 1 distinct chain · 10% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spike glycoprotein	protein	213	10% helix, 40% strand	A0A8E6CMP0

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	344	0.62	0.78	43	empty

Modifications

Observed in the structure: 5 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

7USB · CCoV-HuPn-2018 S in the swung out conformation (local refinement of domain 0) · 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 A0A8E6CMP0
Elsewhere: RCSB PDB 7USB · PDBe 7USB · UniProt A0A8E6CMP0

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