Structure of PDB 3zni Chain I Binding Site BS01
Receptor Information
>3zni Chain I (length=386) Species:
9606
(Homo sapiens) [
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ADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILS
KYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDR
RNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKT
IVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLF
QPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCT
RLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPD
LTGLCEPTPHDHIKVTQEQFELYCEMGSTFQLCKICAENDKDVKIEPCGH
LMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPF
Ligand information
>3zni Chain J (length=8) Species:
9606
(Homo sapiens) [
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DGYTPEPA
Receptor-Ligand Complex Structure
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PDB
3zni
Essentiality of a Non-Ring Element in Priming Donor Ubiquitin for Catalysis by a Monomeric E3.
Resolution
2.21 Å
Binding residue
(original residue number in PDB)
Y266 R286 C289 T290 Y299 Q308 T309 P311 K314 E326 F328 Y329
Binding residue
(residue number reindexed from 1)
Y226 R246 C249 T250 Y259 Q268 T269 P271 K274 E286 F288 Y289
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:3zni
,
PDBe:3zni
,
PDBj:3zni
PDBsum
3zni
PubMed
23851457
UniProt
Q13191
|CBLB_HUMAN E3 ubiquitin-protein ligase CBL-B (Gene Name=CBLB)
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