Structure of PDB 4oti Chain A

Receptor sequence
>4otiA (length=304) Species: 9606 (Homo sapiens) [Search protein sequence]
RKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARD
EVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLML
HIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVK
IADFGLTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR
FLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARR
LPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFD
FVAG
3D structure
PDB4oti Crystal Structures of PRK1 in Complex with the Clinical Compounds Lestaurtinib and Tofacitinib Reveal Ligand Induced Conformational Changes.
ChainA
Resolution1.93 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 MI1 A G628 R629 G630 G633 V635 A648 S704 L753 F910 G17 R18 G19 G22 V24 A37 S93 L142 F268 MOAD: ic50=43nM
PDBbind-CN: -logKd/Ki=7.37,IC50=43nM
BindingDB: Kd=200nM
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:4oti, PDBe:4oti, PDBj:4oti
PDBsum4oti
PubMed25111382
UniProtQ16512|PKN1_HUMAN Serine/threonine-protein kinase N1 (Gene Name=PKN1)

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