Structure of PDB 1fbv Chain A Binding Site BS02
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
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1fbv Chain A Residue 1001 [
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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)
C381 C384 C401 C404
Binding residue
(residue number reindexed from 1)
C335 C338 C355 C358
Annotation score
4
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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