Structure of PDB 1zar Chain A

Receptor sequence
>1zarA (length=267) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence]
NIAELYGKMGKHSWRIMDAIFKNLWDYEYVPLQLISSHARIGEEKARNIL
KYLSDLRVVQNRQKDYEGSTFTFIGLSLYSLHRLVRSGKVDAIGKLMGEG
KESAVFNCYSEKFGECVVKFHKVKVKEHFSVLAIRSARNEFRALQKLQGL
AVPKVYAWEGNAVLMELIDAKELYRVRVENPDEVLDMILEEVAKFYHRGI
VHGDLSQYNVLVSEEGIWIIDFPQSVEVGEEGWREILERDVRNIITYFSR
TYRTEKDINSAIDRILQ
3D structure
PDB1zar Autophosphorylation of Archaeoglobus fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexes.
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
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 MN A N223 D235 N209 D221
BS02 ADP A M98 E103 S104 V118 K120 M179 I182 E186 I234 D235 M97 E102 S103 V117 K119 M165 I168 E172 I220 D221
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
GO:0106310 protein serine kinase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0030490 maturation of SSU-rRNA
Cellular Component
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:1zar, PDBe:1zar, PDBj:1zar
PDBsum1zar
PubMed15943813
UniProtO30245|RIO2_ARCFU RIO-type serine/threonine-protein kinase Rio2 (Gene Name=rio2)

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