MolNFT v1 · #170394 · protein

Structure of maporal virus envelope glycoprotein gc in postfusion conformation

6Y68 · Envelope polyprotein: “Structure of maporal virus envelope glycoprotein gc in postfusion conformation”. X-ray diffraction, 4 ligands (NAG, BMA, MAN), 2 pockets (best druggability 0.53). MolNFT v1 #170394 on GenesisL1: 3D structure…

PDB: 6Y68
Type: protein
Length: 413 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope polyprotein
UniProt: Q5MYC0
Ligands: NAG, BMA, MAN, CD
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Envelope polyprotein	protein	413	5% helix, 54% strand	Q5MYC0

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
BMA · beta-D-mannopyranose · sugar
MAN · alpha-D-mannopyranose · sugar
CD · Cadmium ion · metal · 4 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	199	0.53	0.78	28	empty
2	267	0.51	0.75	33	CD

Modifications

Observed in the structure: 12 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

6Y68 · Structure of Maporal virus envelope glycoprotein 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 Q5MYC0
Elsewhere: RCSB PDB 6Y68 · PDBe 6Y68 · UniProt Q5MYC0

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