Structure of PDB 1yvh Chain A Binding Site BS02
Receptor Information
>1yvh Chain A (length=304) Species:
9606
(Homo sapiens) [
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PGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRT
ILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQP
RRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEK
TIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRL
FQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSC
TRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNP
DLTG
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1yvh Chain A Residue 352 [
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Receptor-Ligand Complex Structure
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PDB
1yvh
Structural Characterization of a Novel Cbl Phosphotyrosine Recognition Motif in the APS Family of Adapter Proteins
Resolution
2.05 Å
Binding residue
(original residue number in PDB)
D229 N233 Y235 E240
Binding residue
(residue number reindexed from 1)
D182 N186 Y188 E193
Annotation score
4
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
PDBsum
1yvh
PubMed
15737992
UniProt
P22681
|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)
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