Structure of PDB 2y1n Chain A

Receptor sequence

>2y1nA (length=377) Species: 9606 (Homo sapiens)

DKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSR
YEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNL
TKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVP
WKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPW
SSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLG
QWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTG
LCEKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSW
QESEGQGCPFCRCEIKGTEPIVVDPFD

3D structure

• PDB: 2y1n Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl.
• Chain: A
• Resolution: 1.999 Å

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 K278 R294 S296 C297 T298 Y307 Q316 T317 P319 E334 F336 Y337	Y223 K227 R243 S245 C246 T247 Y256 Q265 T266 P268 E283 F285 Y286
BS02	ZN	A	C381 C384 C401 C404	C323 C326 C343 C346
BS03	ZN	A	C396 H398 C416 C419	C338 H340 C358 C361
BS04	CA	A	D229 T231 N233 Y235 E240	D178 T180 N182 Y184 E189

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

External links

• PDB: RCSB:2y1n, PDBe:2y1n, PDBj:2y1n
• PDBsum: 2y1n
• PubMed: 22266821
• UniProt: P22681|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)