Structure of PDB 1fbv Chain A Binding Site BS01
Receptor Information
>1fbv Chain A (length=388) Species:
9606
(Homo sapiens) [
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PPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLR
TILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQ
PRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGE
KTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTR
LFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLS
CTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQN
PDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPC
GHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPF
Ligand information
>1fbv Chain B (length=9) Species:
9606
(Homo sapiens) [
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SDGYTPEPA
Receptor-Ligand Complex Structure
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PDB
1fbv
Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.
Resolution
2.9 Å
Binding residue
(original residue number in PDB)
Y83 Y274 R294 C297 T298 Y307 Q316 T317 I318 P319 F336 Y337
Binding residue
(residue number reindexed from 1)
Y37 Y228 R248 C251 T252 Y261 Q270 T271 I272 P273 F290 Y291
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
GO:0046872
metal ion binding
Biological Process
GO:0007166
cell surface receptor signaling pathway
GO:0023051
regulation of signaling
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:1fbv
,
PDBe:1fbv
,
PDBj:1fbv
PDBsum
1fbv
PubMed
10966114
UniProt
P22681
|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)
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