Structure of PDB 4otg Chain A

Receptor sequence
>4otgA (length=324) Species: 9606 (Homo sapiens) [Search protein sequence]
LRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVAR
DEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLM
LHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV
KIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVL
LYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNP
ERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLFTGEAPTLS
PPRDARPLTAAEQAAFLDFDFVAG
3D structure
PDB4otg Crystal Structures of PRK1 in Complex with the Clinical Compounds Lestaurtinib and Tofacitinib Reveal Ligand Induced Conformational Changes.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D746 K748 D750 N751 D764 T784
Catalytic site (residue number reindexed from 1) D136 K138 D140 N141 D154 T174
Enzyme Commision number 2.7.11.13: protein kinase C.
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 2V9 A L627 G628 F632 V635 A648 Y703 S704 G707 L753 L17 G18 F22 V25 A38 Y93 S94 G97 L143 PDBbind-CN: -logKd/Ki=7.59,IC50=26nM
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:4otg, PDBe:4otg, PDBj:4otg
PDBsum4otg
PubMed25111382
UniProtQ16512|PKN1_HUMAN Serine/threonine-protein kinase N1 (Gene Name=PKN1)

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