Structure of PDB 3vrr Chain A

Receptor sequence
>3vrrA (length=291) Species: 9606 (Homo sapiens) [Search protein sequence]
EEARALGRAVRMLQRLEEQCVDVSPPSLRDLLPRTAQLLREVAHSRRAGG
PGGPGGSGDFLLIYLANLEAKSRQVAALLPPRELFRAGSRLRRQLAKLAI
IFSHMHAELHALFPGGKYCGHMYQLTKAPAHTFWRESCGARCVLPWAEFE
SLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLK
NWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRLSCTRLGQWAIG
YVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGKTHNP
3D structure
PDB3vrr Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide A S40 P41 Y244 R264 C267 T268 Y277 Q286 T287 I288 F306 S24 P25 Y218 R238 C241 T242 Y251 Q260 T261 I262 F280
BS02 CA A D199 T201 S203 H205 E210 D173 T175 S177 H179 E184
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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