Structure of PDB 3rwp Chain A

Receptor sequence
>3rwpA (length=278) Species: 9606 (Homo sapiens) [Search protein sequence]
QPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKEN
KVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIR
KIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQIT
DFGTAKVLSSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPP
FRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEME
GYGPLKAHPFFESVTWENLHQQTPPKLT
3D structure
PDB3rwp Discovery of Novel, Potent, and Selective Inhibitors of 3-Phosphoinositide-Dependent Kinase (PDK1).
ChainA
Resolution1.92 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 T164
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 ABQ A L88 G89 E90 G91 T95 V96 A109 K111 A162 E166 E209 L212 T222 D223 L16 G17 E18 G19 T23 V24 A37 K39 A90 E94 E137 L140 T150 D151 MOAD: Ki=0.6nM
PDBbind-CN: -logKd/Ki=9.22,Ki=0.6nM
BindingDB: Ki=0.600000nM
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:3rwp, PDBe:3rwp, PDBj:3rwp
PDBsum3rwp
PubMed22040023
UniProtO15530|PDPK1_HUMAN 3-phosphoinositide-dependent protein kinase 1 (Gene Name=PDPK1)

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