Structure of PDB 1yvh Chain A Binding Site BS02

Receptor Information
>1yvh Chain A (length=304) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRT
ILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQP
RRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEK
TIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRL
FQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSC
TRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNP
DLTG
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1yvh Chain A Residue 352 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1yvh Structural Characterization of a Novel Cbl Phosphotyrosine Recognition Motif in the APS Family of Adapter Proteins
Resolution2.05 Å
Binding residue
(original residue number in PDB)
D229 N233 Y235 E240
Binding residue
(residue number reindexed from 1)
D182 N186 Y188 E193
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
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:1yvh, PDBe:1yvh, PDBj:1yvh
PDBsum1yvh
PubMed15737992
UniProtP22681|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)

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