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Structural basis for variation in adenovirus affinity for the cellular receptor car (S489Y mutant)

Analyse Structural basis for variation in adenovirus affinity for the cellular receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1P6A
Type
protein
Length
309 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fiber protein; Coxsackievirus and adenovirus receptor
UniProt
P36711, P78310
Pockets
2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFiber proteinprotein18510% helix, 41% strandP36711
BCoxsackievirus and adenovirus receptorprotein1247% helix, 47% strandP78310

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11490.440.7519empty
21550.430.7425empty

Interfaces

1 interface between chains.

  • A–B · 821 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1P6A · Structural basis for variation in adenovirus affinity for the cellular receptor car… · the same entry in another collection · chain A against A, TM-score 1.00
  • P78310 · AlphaFold monomer V2.0 prediction for coxsackievirus and adenovirus receptor (P78310) · a predicted model of the same protein · chain B against A, TM-score 0.94

Analyse

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