Structure of PDB 2y1n Chain A Binding Site BS03

Receptor Information

>2y1n Chain A (length=377) Species: 9606 (Homo sapiens)

DKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSR
YEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNL
TKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVP
WKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPW
SSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLG
QWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTG
LCEKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSW
QESEGQGCPFCRCEIKGTEPIVVDPFD

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 2y1n Chain A Residue 1437

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2y1n Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl.
• Resolution: 1.999 Å
• Binding residue (original residue number in PDB): C396 H398 C416 C419
• Binding residue (residue number reindexed from 1): C338 H340 C358 C361
• Annotation score: 4

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

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)