Structure of PDB 4oth Chain A

Receptor sequence
>4othA (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
RKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARD
EVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLML
HIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVK
IADFGLCKTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRY
PRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLA
RRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLD
FDFVAG
3D structure
PDB4oth Crystal Structures of PRK1 in Complex with the Clinical Compounds Lestaurtinib and Tofacitinib Reveal Ligand Induced Conformational Changes.
ChainA
Resolution1.8 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
Catalytic site (residue number reindexed from 1) D135 K137 D139 N140 D153
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 DRN A G628 F632 A648 K650 M701 S704 D708 D750 L753 A763 D764 F910 G17 F21 A37 K39 M90 S93 D97 D139 L142 A152 D153 F270 MOAD: ic50=9nM
PDBbind-CN: -logKd/Ki=8.05,IC50=9nM
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:4oth, PDBe:4oth, PDBj:4oth
PDBsum4oth
PubMed25111382
UniProtQ16512|PKN1_HUMAN Serine/threonine-protein kinase N1 (Gene Name=PKN1)

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