Structure of PDB 4l44 Chain A

Receptor sequence
>4l44A (length=321) Species: 9606 (Homo sapiens) [Search protein sequence]
RGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMI
VRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGEL
FMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQG
HVKLTDFGLCKESIHHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYD
MLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASR
LGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQDSKF
TRQTSESANQVFLGFAYVAPS
3D structure
PDB4l44 Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D195 K197 E199 N200 D213 T233
Catalytic site (residue number reindexed from 1) D138 K140 E142 N143 D156 T171
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 5FI A K76 G77 G80 V82 A98 K100 L102 Y151 L152 M202 D213 K218 K19 G20 G23 V25 A41 K43 L45 Y94 L95 M145 D156 K161 BindingDB: Ki=20nM,IC50=160nM
BS02 ZN A C217 H222 H228 C231 C160 H165 H166 C169
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4l44, PDBe:4l44, PDBj:4l44
PDBsum4l44
PubMed23731517
UniProtP23443|KS6B1_HUMAN Ribosomal protein S6 kinase beta-1 (Gene Name=RPS6KB1)

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