Structure of PDB 1oky Chain A

Receptor sequence
>1okyA (length=282) Species: 9606 (Homo sapiens) [Search protein sequence]
PQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKE
NKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYI
RKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQI
TDFGTAKVLSPANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVA
GLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGC
EEMEGYGPLKAHPFFESVTWENLHQQTPPKLT
3D structure
PDB1oky Structural Basis for Ucn-01 (7-Hydroxystaurosporine) Specificity and Pdk1 (3-Phosphoinositide-Dependent Protein Kinase-1) Inhibition
ChainA
Resolution2.3 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) D134 K136 E138 N139 D152 T168
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 STU A L88 G89 V96 A109 K111 Y161 A162 G165 E166 E209 L212 T222 L17 G18 V25 A38 K40 Y90 A91 G94 E95 E138 L141 T151 MOAD: ic50=6.5nM
PDBbind-CN: -logKd/Ki=8.19,IC50=6.5nM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1oky, PDBe:1oky, PDBj:1oky
PDBsum1oky
PubMed12892559
UniProtO15530|PDPK1_HUMAN 3-phosphoinositide-dependent protein kinase 1 (Gene Name=PDPK1)

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