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Cryo-EM structure of human parainfluenza virus type 3 (HPIV3) in complex with antibody PIA174

Analyse Cryo-EM structure of human parainfluenza virus type 3 (HPIV3) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6MJZ
Type
protein
Length
1,477 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fusion glycoprotein F0; PIA174 Fab heavy chain; PIA174 Fab light chain
UniProt
A0A059QA82
Pockets
20 · best druggability 0.87

Structure

electron microscopy · 5 distinct chains · 26% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFusion glycoprotein F0protein42630% helix, 16% strandA0A059QA82
BFusion glycoprotein F0protein40834% helix, 17% strandA0A059QA82
CFusion glycoprotein F0protein41529% helix, 15% strandA0A059QA82
HPIA174 Fab heavy chainprotein1203% helix, 40% strand—
LPIA174 Fab light chainprotein1080% helix, 31% strand—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18910.870.89111empty
27990.790.8296empty
39900.790.80124empty
42730.760.8832empty
51130.740.9429empty

Interfaces

9 interfaces between chains.

  • A–B · 1682 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 1616 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 1493 Ų buried · 8 hydrogen bonds · protein-protein
  • H–L · 989 Ų buried · 10 hydrogen bonds · protein-protein
  • C–L · 335 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

  • 6MJZ · Cryo-EM structure of Human Parainfluenza Virus Type 3 (hPIV3) in complex with antibody… · the same entry in another collection · chain A against A, TM-score 1.00

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