Structure of PDB 1fbv Chain A

Receptor sequence
>1fbvA (length=388) Species: 9606 (Homo sapiens) [Search protein sequence]
PPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLR
TILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQ
PRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGE
KTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTR
LFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLS
CTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQN
PDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPC
GHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPF
3D structure
PDB1fbv Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.
ChainA
Resolution2.9 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 Y83 Y274 R294 C297 T298 Y307 Q316 T317 I318 P319 F336 Y337 Y37 Y228 R248 C251 T252 Y261 Q270 T271 I272 P273 F290 Y291
BS02 ZN A C381 C384 C401 C404 C335 C338 C355 C358
BS03 ZN A C396 H398 C416 C350 H352 C370
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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