Structure of PDB 3zni Chain M Binding Site BS01
Receptor Information
>3zni Chain M (length=390) Species:
9606
(Homo sapiens) [
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QAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRL
ILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQS
QDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFG
DKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFT
RLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRL
SCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSY
NPDLTGLCEPTPHDHIKVTQEQFELYCEMGSTFQLCKICAENDKDVKIEP
CGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFD
Ligand information
>3zni Chain N (length=9) Species:
9606
(Homo sapiens) [
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SDGYTPEPA
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 S288 C289 T290 Q308 T309 I310 P311 E326 F328 Y329
Binding residue
(residue number reindexed from 1)
Y229 R249 S251 C252 T253 Q271 T272 I273 P274 E289 F291 Y292
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
View graph for
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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