Structure of PDB 2y1n Chain A Binding Site BS01

Receptor Information
>2y1n Chain A (length=377) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSR
YEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNL
TKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVP
WKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPW
SSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLG
QWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTG
LCEKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSW
QESEGQGCPFCRCEIKGTEPIVVDPFD
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2y1n Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl.
Resolution1.999 Å
Binding residue
(original residue number in PDB)		Y274 K278 R294 S296 C297 T298 Y307 Q316 T317 P319 E334 F336 Y337
Binding residue
(residue number reindexed from 1)		Y223 K227 R243 S245 C246 T247 Y256 Q265 T266 P268 E283 F285 Y286
Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
Gene Ontology
Molecular Function
GO:0001784 phosphotyrosine residue binding
GO:0004842 ubiquitin-protein transferase activity
GO:0005509 calcium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0007166 cell surface receptor signaling pathway
GO:0023051 regulation of signaling

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Molecular Function
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Biological Process
External links
PDB RCSB:2y1n, PDBe:2y1n, PDBj:2y1n
PDBsum2y1n
PubMed22266821
UniProtP22681|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)

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