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Coupling of folding and binding in the ptb domain of the signaling protein shc

Analyse Coupling of folding and binding in the ptb domain of the signaling protein shc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OY2
Type
protein
Length
191 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Shc transforming protein
UniProt
P29353
Pockets
3 · best druggability 0.69

Structure

solution nmr · 1 distinct chain · 14% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AShc transforming proteinprotein19114% helix, 20% strandP29353

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13340.690.8246empty
21210.630.8726empty
3570.300.7614empty

Compared structures

  • 1OY2 · Coupling of Folding and Binding in the PTB Domain of the Signaling Protein Shc · the same entry in another collection · chain A against A, TM-score 1.00
  • P29353 · AlphaFold monomer V2.0 prediction for shc-transforming protein 1 (P29353) · a predicted model of the same protein · chain A against A, TM-score 0.66

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