Structure of PDB 4gyi Chain A Binding Site BS02

Receptor Information
>4gyi Chain A (length=339) Species: 759272 (Thermochaetoides thermophila DSM 1495) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLDTRAMRHLTAEDWRVLTAVEMGSKNHEIVPTPLIEKIARLRGGSSGVH
KSIATLAKAGLIARMKEAKYDGYRLTYGGLDYLALHTHAARKDVYSVGSR
IGVGKESDIMIVADEKGKQKVLKIHRLGRISFRTVKRDYLRNRSTGSWMY
LSRLAAIKEFAFMKALYEEGFPVPEPIAQSRHTIVMSLVDALPMRQVSSV
PDPASLYADLIALILRLAKHGLIHGDFNEFNILIREEKDAEDPSSITLTP
IIIDFPQMVSMDHPNAEMYFDRDVQCIKRFFERRFHFVSTTPGPFYKDAK
KTVGKDGAKRLDAALEASGFTKKMAKDLEAAIREQQESR
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain4gyi Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4gyi ATPase-dependent role of the atypical kinase Rio2 on the evolving pre-40S ribosomal subunit.
Resolution2.2 Å
Binding residue
(original residue number in PDB)
N234 X257
Binding residue
(residue number reindexed from 1)
N231 X254
Annotation score1
Enzymatic activity
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:0005524 ATP binding
GO:0044024 histone H2AS1 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0030490 maturation of SSU-rRNA
Cellular Component
GO:0005634 nucleus
GO:0005829 cytosol
GO:0030688 preribosome, small subunit precursor

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4gyi, PDBe:4gyi, PDBj:4gyi
PDBsum4gyi
PubMed23104056
UniProtG0S5R3

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