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Solution structure of the VAV1 SH2 domain complexed with a syk-derived doubly phosphorylated peptide

Analyse Solution structure of the VAV1 SH2 domain complexed with a syk-derived doubly… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2LCT
Type
protein
Length
120 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Proto-oncogene vav; Tyrosine-protein kinase syk
EC
2.7.10.2
UniProt
P15498, P48025

Structure

solution nmr · 2 distinct chains · 18% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProto-oncogene vavprotein10721% helix, 27% strandP15498
BTyrosine-protein kinase syk (EC 2.7.10.2)protein130% helix, 0% strandP48025

Interfaces

1 interface between chains.

  • A–B · 645 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

  • 2LCT · Solution structure of the Vav1 SH2 domain complexed with a Syk-derived doubly… · the same entry in another collection · chain A against A, TM-score 1.00
  • P15498 · AlphaFold monomer V2.0 prediction for proto-oncogene vav (P15498) · a predicted model of the same protein · chain A against A, TM-score 0.84
  • P48025 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase syk (P48025) · a predicted model of the same protein · chain B against A, TM-score 0.30

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