Structure of PDB 1fbv Chain A Binding Site BS01

Receptor Information
>1fbv Chain A (length=388) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLR
TILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQ
PRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGE
KTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTR
LFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLS
CTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQN
PDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPC
GHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPF
Ligand information
Receptor-Ligand Complex Structure
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PDB1fbv Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.
Resolution2.9 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

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Molecular Function

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Biological Process
External links
PDB RCSB:1fbv, PDBe:1fbv, PDBj:1fbv
PDBsum1fbv
PubMed10966114
UniProtP22681|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)

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