Structure of PDB 5fqd Chain C Binding Site BS01

Receptor Information
>5fqd Chain C (length=294) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLY
ESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFT
MKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFG
LAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGY
VLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMY
LNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQ
Ligand information
Ligand IDLVY
InChIInChI=1S/C13H13N3O3/c14-9-3-1-2-7-8(9)6-16(13(7)19)10-4-5-11(17)15-12(10)18/h1-3,10H,4-6,14H2,(H,15,17,18)/t10-/m0/s1
InChIKeyGOTYRUGSSMKFNF-JTQLQIEISA-N
SMILES
SoftwareSMILES
CACTVS 3.385Nc1cccc2C(=O)N(Cc12)[C@H]3CCC(=O)NC3=O
OpenEye OEToolkits 1.9.2c1cc2c(c(c1)N)CN(C2=O)C3CCC(=O)NC3=O
OpenEye OEToolkits 1.9.2c1cc2c(c(c1)N)CN(C2=O)[C@H]3CCC(=O)NC3=O
ACDLabs 12.01O=C1NC(=O)CCC1N3C(=O)c2cccc(c2C3)N
CACTVS 3.385Nc1cccc2C(=O)N(Cc12)[CH]3CCC(=O)NC3=O
FormulaC13 H13 N3 O3
NameS-Lenalidomide
ChEMBL
DrugBank
ZINCZINC000001997127
PDB chain5fqd Chain B Residue 1438 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5fqd Structural Basis of Lenalidomide-Induced Ck1Alpha Degradation by the Crl4(Crbn) Ubiquitin Ligase.
Resolution2.45 Å
Binding residue
(original residue number in PDB)		N39 G40
Binding residue
(residue number reindexed from 1)		N30 G31
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D136 K138
Catalytic site (residue number reindexed from 1) D127 K129
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0044024 histone H2AS1 kinase activity
GO:0106310 protein serine kinase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0007030 Golgi organization
GO:0007165 signal transduction
GO:0007166 cell surface receptor signaling pathway
GO:0016055 Wnt signaling pathway
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0019082 viral protein processing
GO:0031670 cellular response to nutrient
GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0035025 positive regulation of Rho protein signal transduction
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045104 intermediate filament cytoskeleton organization
GO:0051301 cell division
GO:0090090 negative regulation of canonical Wnt signaling pathway
GO:1900226 negative regulation of NLRP3 inflammasome complex assembly
GO:1904263 positive regulation of TORC1 signaling
Cellular Component
GO:0000775 chromosome, centromeric region
GO:0000776 kinetochore
GO:0005634 nucleus
GO:0005694 chromosome
GO:0005737 cytoplasm
GO:0005813 centrosome
GO:0005819 spindle
GO:0005829 cytosol
GO:0005847 mRNA cleavage and polyadenylation specificity factor complex
GO:0005856 cytoskeleton
GO:0005929 cilium
GO:0016020 membrane
GO:0016607 nuclear speck
GO:0030877 beta-catenin destruction complex
GO:0036064 ciliary basal body
GO:0042995 cell projection
GO:0045095 keratin filament

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5fqd, PDBe:5fqd, PDBj:5fqd
PDBsum5fqd
PubMed26909574
UniProtP48729|KC1A_HUMAN Casein kinase I isoform alpha (Gene Name=CSNK1A1)

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