Structure of PDB 6y5p Chain A Binding Site BS02

Receptor Information
>6y5p Chain A (length=228) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KSKNPEDVVRRYMQKVKNPPDEDCTICMERLVTASGYEGVLRHKGVRPEL
VGRLGRCGHMYHLLCLVAMYSNGNKDGSLQCPTCKAIYGEKTGTQPPGKM
EFHLIPHSLPGFPDTQTIRIVYDIPTGIQGPEHPNPGKKFTARGFPRHCY
LPNNEKGRKVLRLLITAWERRLIFTIGTSNTTGESDTVVWNEIHHKTEFG
SNLTGHGYPDASYLDNVLAELTAQGVSE
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain6y5p Chain A Residue 708 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6y5p Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases.
Resolution1.74 Å
Binding residue
(original residue number in PDB)
C411 C414 H449 C452
Binding residue
(residue number reindexed from 1)
C24 C27 H62 C65
Annotation score4
Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
Biological Process
GO:0007219 Notch signaling pathway
GO:0016567 protein ubiquitination

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6y5p, PDBe:6y5p, PDBj:6y5p
PDBsum6y5p
PubMed32948590
UniProtQ86Y01|DTX1_HUMAN E3 ubiquitin-protein ligase DTX1 (Gene Name=DTX1)

[Back to BioLiP]