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Canine parvovirus and FAB14 asymmetric reconstruction

Analyse Canine parvovirus and FAB14 asymmetric reconstruction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7M3N
Type
protein
Length
759 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cpv FAB14 light chain; Cpv FAB14 heavy chain; Capsid protein 2
UniProt
B2ZG07
Pockets
12 · best druggability 0.64

Structure

electron microscopy · 3 distinct chains · 6% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LCpv FAB14 light chainprotein1080% helix, 50% strand—
HCpv FAB14 heavy chainprotein1193% helix, 43% strand—
ACapsid protein 2protein5328% helix, 31% strandB2ZG07

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12530.640.8246empty
23780.580.7544empty
34160.560.7436empty
41740.520.7926empty
5680.410.8023empty

Interfaces

3 interfaces between chains.

  • L–H · 828 Ų buried · 7 hydrogen bonds · protein-protein
  • H–A · 422 Ų buried · 3 hydrogen bonds · protein-protein
  • L–A · 219 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 7M3N · Canine parvovirus and Fab14 asymmetric reconstruction · the same entry in another collection · chain L against L, TM-score 1.00

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