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UniProt P29353

P29353

P29353 (UniProt P29353): 17 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P29353
Experimental structures
17
Predicted models
0

Structures

17 records of P29353 in the MolNFT archive: 17 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1MILTransforming proteinx-ray diffractionA——
1MILTransforming proteinx-ray diffractionA——
1N3HCoupling of Folding and Binding in the PTB Domain of the Signaling Protein Shcsolution nmrA——
1N3HCoupling of folding and binding in the ptb domain of the signaling protein shcsolution nmrA——
1OY2Coupling of Folding and Binding in the PTB Domain of the Signaling Protein Shcsolution nmrA——
1OY2Coupling of folding and binding in the ptb domain of the signaling protein shcsolution nmrA——
1QG1Growth factor receptor binding protein SH2 domain complexed with an shc-derived peptidesolution nmrI——
1QG1Growth factor receptor binding protein SH2 domain complexed with an shc-derived peptidesolution nmrI——
1SHCShc ptb domain complexed with a trka receptor phosphopeptide, NMR, minimized average structuresolution nmrA——
1SHCShc ptb domain complexed with a trka receptor phosphopeptide, NMR, minimized average structuresolution nmrA——
1TCESolution NMR structure of the shc SH2 domain complexed with a tyrosine-phosphorylated peptide from…solution nmrA——
1TCESolution NMR structure of the shc SH2 domain complexed with a tyrosine-phosphorylated peptide from…solution nmrA——
4JMHCrystal structure of synthetic protein in complex with double pY peptidex-ray diffractionB——
4JMHCrystal structure of synthetic protein in complex with double py peptidex-ray diffractionB——
4XWXCrystal structure of the PTB domain of SHCx-ray diffractionA——
4XWXCrystal structure of the ptb domain of shcx-ray diffractionA——
P29353AlphaFold monomer V2.0 prediction for shc-transforming protein 1 (P29353)———

Elsewhere

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