Structure of PDB 5ack Chain A

Receptor sequence
>5ackA (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
QPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKEN
KVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIR
KIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQIT
DFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCII
YQLVAGLPPFRAGNEGLIFAKIIKLEYDFPEKFFPKARDLVEKLLVLDAT
KRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT
3D structure
PDB5ack Discovery of a Potent Allosteric Kinase Modulator by Combining Computational and Synthetic Methods.
ChainA
Resolution1.24 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D205 K207 E209 N210 D223 T245
Catalytic site (residue number reindexed from 1) D133 K135 E137 N138 D151 T173
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 ATP A G89 G91 S94 V96 S160 Y161 A162 E166 L212 G17 G19 S22 V24 S88 Y89 A90 E94 L140
BS02 SVQ A K115 I118 I119 V127 R131 T148 F149 Q150 L155 F157 K43 I46 I47 V55 R59 T76 F77 Q78 L83 F85
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:5ack, PDBe:5ack, PDBj:5ack
PDBsum5ack
PubMed26385475
UniProtO15530|PDPK1_HUMAN 3-phosphoinositide-dependent protein kinase 1 (Gene Name=PDPK1)

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