Structure of PDB 3vro Chain A Binding Site BS01

Receptor Information
>3vro Chain A (length=284) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EEARALGRAVRMLQRLEEQCVVSPPSLRDLLPRTAQLLREVAHSRRAGGP
GGPGGSGDFLLIYLANLEAKSRQVAALLSRLRRQLAKLAIIFSHMHAELH
ALFPGGKYCGHMYQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVE
PGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLKNWQLLAVNHP
GYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQ
TIPANKPLSQVLLEGQKDGFYLYPDGKTHNPDLT
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3vro Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		S40 P41 Y244 R264 S266 C267 T268 Q286 T287 I288
Binding residue
(residue number reindexed from 1)		S23 P24 Y208 R228 S230 C231 T232 Q250 T251 I252
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:3vro, PDBe:3vro, PDBj:3vro
PDBsum3vro
PubMed22888118
UniProtQ9ULV8|CBLC_HUMAN E3 ubiquitin-protein ligase CBL-C (Gene Name=CBLC)

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