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Structure of hantavirus envelope glycoprotein gc in complex with scfv A5

Analyse Structure of hantavirus envelope glycoprotein gc in complex with scfv A5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LJY
Type
protein
Length
594 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Envelopment polyprotein; SCFVA5
UniProt
P08668
Ligands
NCO, NAG
Pockets
5 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 4% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEnvelopment polyproteinprotein3744% helix, 60% strandP08668
HSCFVA5protein1130% helix, 49% strand—
LSCFVA5protein1077% helix, 48% strand—

Ligands and binding sites

  • NCO · Cobalt hexammine(iii) · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1880.640.9021empty
2810.420.7918empty
3970.390.7719empty
4540.350.7915empty
5510.340.7815empty

Interfaces

3 interfaces between chains.

  • H–L · 699 Ų buried · 7 hydrogen bonds · protein-protein
  • A–L · 678 Ų buried · 7 hydrogen bonds · protein-protein
  • A–H · 471 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 5LJY · Structure of hantavirus envelope glycoprotein Gc in complex with scFv A5 · the same entry in another collection · chain A against A, TM-score 1.00

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