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Cryoem structure of rhinovirus B14 in complex with C5 Fab (33 degrees celsius, molar ratio 1:3, empty particle)

Analyse Cryoem structure of rhinovirus B14 in complex with C5 Fab (33 degrees celsius… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5W3O
Type
protein
Length
901 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
C5 antibody variable heavy domain; C5 antibody variable light domain; Viral protein 1…
UniProt
P03303
Pockets
12 · best druggability 0.76

Structure

electron microscopy · 5 distinct chains · 8% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
DC5 antibody variable heavy domainprotein1163% helix, 43% strand—
EC5 antibody variable light domainprotein1070% helix, 45% strand—
AViral protein 1protein2299% helix, 32% strandP03303
BViral protein 3protein2159% helix, 32% strandP03303
CViral protein 2protein23412% helix, 34% strandP03303

Pockets

12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.760.9726empty
21890.720.8924empty
33880.670.8047empty
41320.470.7827empty
51180.450.7820empty

Interfaces

9 interfaces between chains.

  • A–B · 2812 Ų buried · 50 hydrogen bonds · protein-protein
  • A–C · 1750 Ų buried · 33 hydrogen bonds · protein-protein
  • B–C · 1472 Ų buried · 13 hydrogen bonds · protein-protein
  • D–E · 877 Ų buried · 6 hydrogen bonds · protein-protein
  • E–B · 421 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 5W3O · CryoEM structure of rhinovirus B14 in complex with C5 Fab (33 degrees Celsius, molar… · the same entry in another collection · chain D against D, TM-score 1.00

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