Structure of PDB 3vrr Chain A Binding Site BS02

Receptor Information
>3vrr Chain A (length=291) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EEARALGRAVRMLQRLEEQCVDVSPPSLRDLLPRTAQLLREVAHSRRAGG
PGGPGGSGDFLLIYLANLEAKSRQVAALLPPRELFRAGSRLRRQLAKLAI
IFSHMHAELHALFPGGKYCGHMYQLTKAPAHTFWRESCGARCVLPWAEFE
SLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLK
NWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRLSCTRLGQWAIG
YVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGKTHNP
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain3vrr Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3vrr Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
Resolution2.0 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 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:3vrr, PDBe:3vrr, PDBj:3vrr
PDBsum3vrr
PubMed22888118
UniProtQ9ULV8|CBLC_HUMAN E3 ubiquitin-protein ligase CBL-C (Gene Name=CBLC)

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