Structure of PDB 2y1n Chain C Binding Site BS02

Receptor Information
>2y1n Chain C (length=380) 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
LCEDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCL
TSWQESEGQGCPFCRCEIKGTEPIVVDPFD
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain2y1n Chain C Residue 1436 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)
C381 C384 C401 C404
Binding residue
(residue number reindexed from 1)
C326 C329 C346 C349
Annotation score4
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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