Structure of PDB 6yid Chain C

Receptor sequence
>6yidC (length=259) Species: 9606 (Homo sapiens) [Search protein sequence]
GGSMEVVGDFEYSKRDLVGHGAFAVVFRGRHRQKTDWEVAIKSINKKNLS
KSQILLGKEIKILKELQHENIVALYDVQELPNSVFLVMEYCNGGDLADYL
QAKGTLSEDTIRVFLHQIAAAMRILHSKGIIHRDLKPQNILLSYANGIRI
KIADFGFARYLHSSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPP
FQANSPQDLRMFYEKNRSLMPSIPRETSPYLANLLLGLLQRNQKDRMDFE
AFFSHPFLE
3D structure
PDB6yid Design, Synthesis, and Characterization of an Orally Active Dual-Specific ULK1/2 Autophagy Inhibitor that Synergizes with the PARP Inhibitor Olaparib for the Treatment of Triple-Negative Breast Cancer.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D131 K133 Q135 N136 D158 S177
Catalytic site (residue number reindexed from 1) D134 K136 Q138 N139 D154 S164
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
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 EDJ C V15 V23 A37 C88 G91 V18 V26 A40 C91 G94 BindingDB: IC50=711nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0010506 regulation of autophagy

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6yid, PDBe:6yid, PDBj:6yid
PDBsum6yid
PubMed33200929
UniProtQ8IYT8|ULK2_HUMAN Serine/threonine-protein kinase ULK2 (Gene Name=ULK2)

[Back to BioLiP]