Structure of PDB 5mrd Chain A

Receptor sequence
>5mrdA (length=284) Species: 9606 (Homo sapiens) [Search protein sequence]
SKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKIVEKRHVNKENKIP
YVQREKDVMSRLDHPFFVKLYFCFQDDEKLYFGLSYAKNGELLKYIRKIG
SFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFG
TAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQL
VAGLPPFRAGNEGLIFAKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRL
GCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT
3D structure
PDB5mrd An Allosteric Inhibitor Scaffold Targeting the PIF-Pocket of Atypical Protein Kinase C Isoforms.
ChainA
Resolution1.41 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) D130 K132 E134 N135 D148 T170
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 S26 A K115 N119 Q128 K131 L155 F157 K40 N44 Q53 K56 L80 F82 MOAD: ic50=36.4uM
PDBbind-CN: -logKd/Ki=4.44,IC50=36.4uM
BS02 ATP A G89 V96 K111 Y126 S160 A162 E166 L212 G14 V21 K36 Y51 S85 A87 E91 L137
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:5mrd, PDBe:5mrd, PDBj:5mrd
PDBsum5mrd
PubMed28045490
UniProtO15530|PDPK1_HUMAN 3-phosphoinositide-dependent protein kinase 1 (Gene Name=PDPK1)

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