Structure of PDB 2y1n Chain C Binding Site BS01
Receptor Information
>2y1n Chain C (length=380) Species:
9606
(Homo sapiens) [
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DKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSR
YEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNL
TKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVP
WKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPW
SSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLG
QWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTG
LCEDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCL
TSWQESEGQGCPFCRCEIKGTEPIVVDPFD
Ligand information
>2y1n Chain D (length=9) Species:
9606
(Homo sapiens) [
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SDGYTPEPA
Receptor-Ligand Complex Structure
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PDB
2y1n
Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl.
Resolution
1.999 Å
Binding residue
(original residue number in PDB)
Y274 K278 R294 S296 C297 T298 Q316 T317 I318 P319 E334 F336 Y337
Binding residue
(residue number reindexed from 1)
Y223 K227 R243 S245 C246 T247 Q265 T266 I267 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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:2y1n
,
PDBe:2y1n
,
PDBj:2y1n
PDBsum
2y1n
PubMed
22266821
UniProt
P22681
|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)
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