Structure of PDB 3vrr Chain A Binding Site BS02
Receptor Information
>3vrr Chain A (length=291) Species:
9606
(Homo sapiens) [
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EEARALGRAVRMLQRLEEQCVDVSPPSLRDLLPRTAQLLREVAHSRRAGG
PGGPGGSGDFLLIYLANLEAKSRQVAALLPPRELFRAGSRLRRQLAKLAI
IFSHMHAELHALFPGGKYCGHMYQLTKAPAHTFWRESCGARCVLPWAEFE
SLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLK
NWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRLSCTRLGQWAIG
YVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGKTHNP
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
3vrr Chain A Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
3vrr
Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
D199 T201 S203 H205 E210
Binding residue
(residue number reindexed from 1)
D173 T175 S177 H179 E184
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:3vrr
,
PDBe:3vrr
,
PDBj:3vrr
PDBsum
3vrr
PubMed
22888118
UniProt
Q9ULV8
|CBLC_HUMAN E3 ubiquitin-protein ligase CBL-C (Gene Name=CBLC)
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