Structure of PDB 5j3x Chain E

Receptor sequence
>5j3xE (length=381) Species: 9606 (Homo sapiens) [Search protein sequence]
VDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILS
RYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRN
LTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIV
PWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQP
WSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRL
GQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLT
GLCEDHIKVTQEQYELFCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSC
LTSWQESEGQGCPFCRCEIKGTEPIVVDPFD
3D structure
PDB5j3x Casitas B-lineage lymphoma linker helix mutations found in myeloproliferative neoplasms affect conformation.
ChainE
Resolution2.822 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 ZN E C381 C384 C401 C404 C327 C330 C347 C350
BS02 ZN E C396 H398 C416 C419 C342 H344 C362 C365
BS03 CA E D229 T231 N233 Y235 E240 D179 T181 N183 Y185 E190
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:5j3x, PDBe:5j3x, PDBj:5j3x
PDBsum5j3x
PubMed27609087
UniProtP22681|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)

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