Structure of PDB 4a4b Chain A

Receptor sequence
>4a4bA (length=388) Species: 9606 (Homo sapiens) [Search protein sequence]
PGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRT
ILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQP
RRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEK
TIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRL
FQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSC
TRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNP
DLTGLCEPTPQDHIKVTQEQFELYCEMGSTFQLCKICAENDKDVKIEPCG
HLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFD
3D structure
PDB4a4b Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl
ChainA
Resolution2.789 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 Y274 R294 S296 C297 T298 Y307 Q316 T317 P319 F336 Y337 Y227 R247 S249 C250 T251 Y260 Q269 T270 P272 F289 Y290
BS02 ZN A C381 C384 C401 C404 C334 C337 C354 C357
BS03 ZN A C396 H398 C416 C419 C349 H351 C369 C372
BS04 CA A D229 T231 N233 Y235 E240 D182 T184 N186 Y188 E193
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:4a4b, PDBe:4a4b, PDBj:4a4b
PDBsum4a4b
PubMed22266821
UniProtP22681|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)

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