Structure of PDB 4a07 Chain A

Receptor sequence
>4a07A (length=284) Species: 9606 (Homo sapiens) [Search protein sequence]
KKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVP
YVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIG
SFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFG
TAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQL
VAGLPPFRAGNEGLIFAKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRL
GCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT
3D structure
PDB4a07 Allosteric Regulation of Protein Kinase Pkczeta by the N-Terminal C1 Domain and Small Compounds to the Pif-Pocket.
ChainA
Resolution1.85 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 ATP A G89 G91 S92 S94 V96 A109 K111 A162 E166 L212 G14 G16 S17 S19 V21 A34 K36 A87 E91 L137
BS02 AZ7 A K76 K115 I119 V127 R131 L155 F157 K1 K40 I44 V52 R56 L80 F82
BS03 AZ7 A L168 R172 G278 L279 P280 L93 R97 G203 L204 P205
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:4a07, PDBe:4a07, PDBj:4a07
PDBsum4a07
PubMed22118680
UniProtO15530|PDPK1_HUMAN 3-phosphoinositide-dependent protein kinase 1 (Gene Name=PDPK1)

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