Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T60003 | Target Info | |||
| Target Name | Protein kinase N1 (PKN1) | ||||
| Synonyms | Serine/threonine-protein kinase N1; Serine-threonine protein kinase N; Protein-kinase C-related kinase 1; Protein kinase PKN-alpha; Protein kinase C-like PKN; Protein kinase C-like 1; Protease-activated kinase 1; PRKCL1; PRK1; PKN; PAK1 | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | PKN1 | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Tofacitinib | Ligand Info | |||||
| Structure Description | Crystal Structure of PRK1 Catalytic Domain in Complex with Tofacitinib | PDB:4OTI | ||||
| Method | X-ray diffraction | Resolution | 1.93 Å | Mutation | No | [1] |
| PDB Sequence |
RKSPLTLEDF
621 KFLAVLGRGH631 FGKVLLSEFR641 PSGELFAIKA651 LKKGDIVARD661 EVESLMCEKR 671 ILAAVTSAGH681 PFLVNLFGCF691 QTPEHVCFVM701 EYSAGGDLML711 HIHSDVFSEP 721 RAIFYSACVV731 LGLQFLHEHK741 IVYRDLKLDN751 LLLDTEGYVK761 IADFGLTRAV 802 DWWGLGVLLY812 EMLVGESPFP822 GDDEEEVFDS832 IVNDEVRYPR842 FLSAEAIGIM 852 RRLLRRNPER862 RLGSSERDAE872 DVKKQPFFRT882 LGWEALLARR892 LPPPFVPTLS 902 GRTDVSNFDE912 EFTGEAPTLP923 PRDARPLTAA933 EQAAFLDFDF943 VAG |
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LEU627
3.679
GLY628
3.309
ARG629
3.390
GLY630
3.135
GLY633
3.200
LYS634
3.497
VAL635
3.146
ALA648
3.452
LYS650
3.747
LEU652
4.662
VAL685
3.753
|
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| Ligand Name: Lestaurtinib | Ligand Info | |||||
| Structure Description | Crystal Structure of PRK1 Catalytic Domain in Complex with Lestaurtinib | PDB:4OTG | ||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [1] |
| PDB Sequence |
LRKSPLTLED
620 FKFLAVLGRG630 HFGKVLLSEF640 RPSGELFAIK650 ALKKGDIVAR660 DEVESLMCEK 670 RILAAVTSAG680 HPFLVNLFGC690 FQTPEHVCFV700 MEYSAGGDLM710 LHIHSDVFSE 720 PRAIFYSACV730 VLGLQFLHEH740 KIVYRDLKLD750 NLLLDTEGYV760 KIADFGLCKE 770 GMGYGDRTSF781 CGTPEFLAPE791 VLTDTSYTRA801 VDWWGLGVLL811 YEMLVGESPF 821 PGDDEEEVFD831 SIVNDEVRYP841 RFLSAEAIGI851 MRRLLRRNPE861 RRLGSSERDA 871 EDVKKQPFFR881 TLGWEALLAR891 RLPPPFVPTL901 FTGEAPTLPP924 RDARPLTAAE 934 QAAFLDFDFV944 AG
|
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LEU627
3.528
GLY628
3.271
ARG629
3.749
GLY630
4.785
PHE632
3.546
VAL635
3.587
ALA648
3.426
LYS650
4.083
VAL685
4.136
MET701
4.075
GLU702
2.885
|
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| Ligand Name: L-serine-O-phosphate | Ligand Info | |||||
| Structure Description | Crystal Structure of PRK1 Catalytic Domain in Complex with Ro-31-8220 | PDB:4OTH | ||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [1] |
| PDB Sequence |
RKSPLTLEDF
621 KFLAVLGRGH631 FGKVLLSEFR641 PSGELFAIKA651 LKKGDIVARD661 EVESLMCEKR 671 ILAAVTSAGH681 PFLVNLFGCF691 QTPEHVCFVM701 EYSAGGDLML711 HIHSDVFSEP 721 RAIFYSACVV731 LGLQFLHEHK741 IVYRDLKLDN751 LLLDTEGYVK761 IADFGLCKTR 800 AVDWWGLGVL810 LYEMLVGESP820 FPGDDEEEVF830 DSIVNDEVRY840 PRFLSAEAIG 850 IMRRLLRRNP860 ERRLGSSERD870 AEDVKKQPFF880 RTLGWEALLA890 RRLPPPFVPT 900 LSGRTDVSNF910 DEEFTGEAPT920 LPPRDARPLT931 AAEQAAFLDF941 DFVAG |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SEP or .SEP2 or .SEP3 or :3SEP;style chemicals stick;color identity;select .A:629 or .A:634 or .A:653 or .A:696 or .A:920 or .A:921 or .A:923 or .A:924; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Ro31-8220 | Ligand Info | |||||
| Structure Description | Crystal Structure of PRK1 Catalytic Domain in Complex with Ro-31-8220 | PDB:4OTH | ||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [1] |
| PDB Sequence |
RKSPLTLEDF
621 KFLAVLGRGH631 FGKVLLSEFR641 PSGELFAIKA651 LKKGDIVARD661 EVESLMCEKR 671 ILAAVTSAGH681 PFLVNLFGCF691 QTPEHVCFVM701 EYSAGGDLML711 HIHSDVFSEP 721 RAIFYSACVV731 LGLQFLHEHK741 IVYRDLKLDN751 LLLDTEGYVK761 IADFGLCKTR 800 AVDWWGLGVL810 LYEMLVGESP820 FPGDDEEEVF830 DSIVNDEVRY840 PRFLSAEAIG 850 IMRRLLRRNP860 ERRLGSSERD870 AEDVKKQPFF880 RTLGWEALLA890 RRLPPPFVPT 900 LSGRTDVSNF910 DEEFTGEAPT920 LPPRDARPLT931 AAEQAAFLDF941 DFVAG |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .DRN or .DRN2 or .DRN3 or :3DRN;style chemicals stick;color identity;select .A:627 or .A:628 or .A:632 or .A:635 or .A:648 or .A:650 or .A:685 or .A:701 or .A:702 or .A:703 or .A:704 or .A:707 or .A:708 or .A:750 or .A:751 or .A:753 or .A:763 or .A:764 or .A:909 or .A:910 or .A:914; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU627
3.617
GLY628
3.814
PHE632
3.462
VAL635
3.832
ALA648
3.410
LYS650
3.757
VAL685
3.409
MET701
3.434
GLU702
2.896
TYR703
3.592
SER704
3.018
|
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| Ligand Name: Phosphonothreonine | Ligand Info | |||||
| Structure Description | Crystal Structure of PRK1 Catalytic Domain in Complex with Lestaurtinib | PDB:4OTG | ||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [1] |
| PDB Sequence |
LRKSPLTLED
620 FKFLAVLGRG630 HFGKVLLSEF640 RPSGELFAIK650 ALKKGDIVAR660 DEVESLMCEK 670 RILAAVTSAG680 HPFLVNLFGC690 FQTPEHVCFV700 MEYSAGGDLM710 LHIHSDVFSE 720 PRAIFYSACV730 VLGLQFLHEH740 KIVYRDLKLD750 NLLLDTEGYV760 KIADFGLCKE 770 GMGYGDRTSF781 CGTPEFLAPE791 VLTDTSYTRA801 VDWWGLGVLL811 YEMLVGESPF 821 PGDDEEEVFD831 SIVNDEVRYP841 RFLSAEAIGI851 MRRLLRRNPE861 RRLGSSERDA 871 EDVKKQPFFR881 TLGWEALLAR891 RLPPPFVPTL901 FTGEAPTLPP924 RDARPLTAAE 934 QAAFLDFDFV944 AG
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TPO or .TPO2 or .TPO3 or :3TPO;style chemicals stick;color identity;select .A:745 or .A:769 or .A:778 or .A:779 or .A:781 or .A:782 or .A:792 or .A:798; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Crystal structures of PRK1 in complex with the clinical compounds lestaurtinib and tofacitinib reveal ligand induced conformational changes. PLoS One. 2014 Aug 11;9(8):e103638. | ||||
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