Structure of PDB 2y1m Chain E Binding Site BS03

Receptor Information

>2y1m Chain E (length=383) Species: 9606 (Homo sapiens)

PPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLR
TILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQ
PRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGE
KTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTR
LFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLS
CTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQN
PDLTGLCHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCT
SCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFD

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 2y1m Chain E Residue 1438

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2y1m Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl.
• Resolution: 2.67 Å
• Binding residue (original residue number in PDB): D229 T231 N233 Y235 E240
• Binding residue (residue number reindexed from 1): D183 T185 N187 Y189 E194
• 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:2y1m, PDBe:2y1m, PDBj:2y1m
• PDBsum: 2y1m
• PubMed: 22266821
• UniProt: P22681|CBL_HUMAN E3 ubiquitin-protein ligase CBL (Gene Name=CBL)