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Solution structure of the SH2 domain of csk in complex with a phosphopeptide from cbp

Analyse Solution structure of the SH2 domain of csk in complex with a phosphopeptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2RSY
Type
protein
Length
137 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine-protein kinase csk; Phosphoprotein associated with glycosphingolipid-enriched…
EC
2.7.10.2
UniProt
P32577, Q9JM80

Structure

solution nmr · 2 distinct chains · 17% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-protein kinase csk (EC 2.7.10.2)protein9917% helix, 29% strandP32577
BPhosphoprotein associated with glycosphingolipid-enriched microdomains 1protein3816% helix, 0% strandQ9JM80

Interfaces

1 interface between chains.

  • A–B · 1003 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, phosphorylation).

Compared structures

  • 2RSY · Solution structure of the SH2 domain of Csk in complex with a phosphopeptide from Cbp · the same entry in another collection · chain A against A, TM-score 1.00
  • P32577 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase csk (P32577) · a predicted model of the same protein · chain A against A, TM-score 0.92
  • Q9JM80 · AlphaFold monomer V2.0 prediction for phosphoprotein associated with… · a predicted model of the same protein · chain B against A, TM-score 0.41

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