Structure of PDB 2y1m Chain F

Receptor sequence
>2y1mF (length=384) Species: 9606 (Homo sapiens) [Search protein sequence]
PPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLR
TILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQ
PRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGE
KTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTR
LFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLS
CTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQN
PDLTGLCDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMC
TSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFD
3D structure
PDB2y1m Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl.
ChainF
Resolution2.67 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN F C381 C384 C401 C404 C330 C333 C350 C353
BS02 ZN F C396 H398 C416 C419 C345 H347 C365 C368
BS03 CA F D229 T231 N233 Y235 E240 D183 T185 N187 Y189 E194
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:2y1m, PDBe:2y1m, PDBj:2y1m
PDBsum2y1m
PubMed22266821
UniProtP22681|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)

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