Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T23276 | Target Info | |||
| Target Name | Extracellular signal-regulated kinase 1 (ERK1) | ||||
| Synonyms | PRKM3; P44-MAPK; P44-ERK1; P44 Mitogen-activated protein kinase; Mitogen-activated protein kinase 3; Microtubule-associated protein-2 kinase; Microtubule-associated protein 2 kinase; MAPK 3; MAP kinase isoform p44; MAP kinase 3; Insulin-stimulated MAP2 kinase; ERT2; ERK-1 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | MAPK3 | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: SCH772984 | Ligand Info | |||||
| Structure Description | Structure of human ERK1 in complex with SCH772984 revealing a novel inhibitor-induced binding pocket | PDB:4QTB | ||||
| Method | X-ray diffraction | Resolution | 1.40 Å | Mutation | No | [1] |
| PDB Sequence |
VPGEVEMVKG
33 QPFDVGPRYT43 QLQYIGEGAY53 GMVSSAYDHV63 RKTRVAIKKI73 SPFEHQTYCQ 83 RTLREIQILL93 RFRHENVIGI103 RDILRASTLE113 AMRDVYIVQD123 LMETDLYKLL 133 KSQQLSNDHI143 CYFLYQILRG153 LKYIHSANVL163 HRDLKPSNLL173 INTTCDLKIC 183 DFGLARIADP193 EHDHTGFLTE203 YVATRWYRAP213 EIMLNSKGYT223 KSIDIWSVGC 233 ILAEMLSNRP243 IFPGKHYLDQ253 LNHILGILGS263 PSQEDLNCII273 NMKARNYLQS 283 LPSKTKVAWA293 KLFPKSDSKA303 LDLLDRMLTF313 NPNKRITVEE323 ALAHPYLEQY 333 YDPTDEPVAE343 EPFTFAMELD353 DLPKERLKEL363 IFQETARFQP373 G |
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ILE48
3.903
ALA52
3.076
TYR53
3.374
VAL56
4.321
ALA69
3.490
LYS71
2.924
ILE73
3.555
PRO75
4.605
TYR81
3.222
ARG84
3.581
THR85
3.616
GLU88
3.468
ILE101
4.105
ILE120
4.690
|
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| Ligand Name: 5'-iodotubercidin | Ligand Info | |||||
| Structure Description | Structural dissection of human mitogen-activated kinase ERK1 | PDB:2ZOQ | ||||
| Method | X-ray diffraction | Resolution | 2.39 Å | Mutation | No | [2] |
| PDB Sequence |
VPGEVEMVKG
33 QPFDVGPRYT43 QLQYIGEGAY53 GMVSSAYDHV63 RKTRVAIKKI73 SPFEHQTYCQ 83 RTLREIQILL93 RFRHENVIGI103 RDILRASTLE113 AMRDVYIVQD123 LMETDLYKLL 133 KSQQLSNDHI143 CYFLYQILRG153 LKYIHSANVL163 HRDLKPSNLL173 INTTCDLKIC 183 DFGLARIADP193 EHDHTGFLTE203 VATRWYRAPE214 IMLNSKGYTK224 SIDIWSVGCI 234 LAEMLSNRPI244 FPGKHYLDQL254 NHILGILGSP264 SQEDLNCIIN274 MKARNYLQSL 284 PSKTKVAWAK294 LFPKSDSKAL304 DLLDRMLTFN314 PNKRITVEEA324 LAHPYLEQYY 334 DPTDEPVAEE344 PFTFAMELDD354 LPKERLKELI364 FQETARFQPG374 V |
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| Ligand Name: Phosphonotyrosine | Ligand Info | |||||
| Structure Description | Structural dissection of human mitogen-activated kinase ERK1 | PDB:2ZOQ | ||||
| Method | X-ray diffraction | Resolution | 2.39 Å | Mutation | No | [2] |
| PDB Sequence |
VPGEVEMVKG
33 QPFDVGPRYT43 QLQYIGEGAY53 GMVSSAYDHV63 RKTRVAIKKI73 SPFEHQTYCQ 83 RTLREIQILL93 RFRHENVIGI103 RDILRASTLE113 AMRDVYIVQD123 LMETDLYKLL 133 KSQQLSNDHI143 CYFLYQILRG153 LKYIHSANVL163 HRDLKPSNLL173 INTTCDLKIC 183 DFGLARIADP193 EHDHTGFLTE203 VATRWYRAPE214 IMLNSKGYTK224 SIDIWSVGCI 234 LAEMLSNRPI244 FPGKHYLDQL254 NHILGILGSP264 SQEDLNCIIN274 MKARNYLQSL 284 PSKTKVAWAK294 LFPKSDSKAL304 DLLDRMLTFN314 PNKRITVEEA324 LAHPYLEQYY 334 DPTDEPVAEE344 PFTFAMELDD354 LPKERLKELI364 FQETARFQPG374 V |
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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 .PTR or .PTR2 or .PTR3 or :3PTR;style chemicals stick;color identity;select .A:87 or .A:165 or .A:187 or .A:189 or .A:202 or .A:203 or .A:205 or .A:206 or .A:211 or .A:215 or .A:220 or .A:222 or .A:250; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: N-[2-[[5-chloro-2-[4-(4-methylpiperazin-1-yl)anilino]pyrimidin-4-yl]amino]phenyl]prop-2-enamide | Ligand Info | |||||
| Structure Description | Crystal structure of ERK1 covalently bound to SM1-71 | PDB:6GES | ||||
| Method | X-ray diffraction | Resolution | 2.07 Å | Mutation | No | [3] |
| PDB Sequence |
PGEVEMVKGQ
34 PFDVGPRYTQ44 LQYIGEGAYG54 MVSSAYDHVR64 KTRVAIKKIS74 PFEHQTYCQR 84 TLREIQILLR94 FRHENVIGIR104 DILRASTLEA114 MRDVYIVQDL124 METDLYKLLK 134 SQQLSNDHIC144 YFLYQILRGL154 KYIHSANVLH164 RDLKPSNLLI174 NTTCDLKICD 184 FGLARIADPE194 HDHTGFLTEY204 VATRWYRAPE214 IMLNSKGYTK224 SIDIWSVGCI 234 LAEMLSNRPI244 FPGKHYLDQL254 NHILGILGSP264 SQEDLNCIIN274 MKARNYLQSL 284 PSKTKVAWAK294 LFPKSDSKAL304 DLLDRMLTFN314 PNKRITVEEA324 LAHPYLEQYY 334 DPTDEPVAEE344 PFTFAMELDD354 LPKERLKELI364 FQETARFQPG374 |
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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 .EWH or .EWH2 or .EWH3 or :3EWH;style chemicals stick;color identity;select .A:255 or .A:258 or .A:259 or .A:262 or .A:263 or .A:280 or .A:284 or .A:285 or .A:286 or .A:287; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: N-[2-[[5-chloro-2-[4-(4-methylpiperazin-1-yl)anilino]pyrimidin-4-yl]amino]phenyl]propanamide | Ligand Info | |||||
| Structure Description | Crystal structure of ERK1 covalently bound to SM1-71 | PDB:6GES | ||||
| Method | X-ray diffraction | Resolution | 2.07 Å | Mutation | No | [3] |
| PDB Sequence |
PGEVEMVKGQ
34 PFDVGPRYTQ44 LQYIGEGAYG54 MVSSAYDHVR64 KTRVAIKKIS74 PFEHQTYCQR 84 TLREIQILLR94 FRHENVIGIR104 DILRASTLEA114 MRDVYIVQDL124 METDLYKLLK 134 SQQLSNDHIC144 YFLYQILRGL154 KYIHSANVLH164 RDLKPSNLLI174 NTTCDLKICD 184 FGLARIADPE194 HDHTGFLTEY204 VATRWYRAPE214 IMLNSKGYTK224 SIDIWSVGCI 234 LAEMLSNRPI244 FPGKHYLDQL254 NHILGILGSP264 SQEDLNCIIN274 MKARNYLQSL 284 PSKTKVAWAK294 LFPKSDSKAL304 DLLDRMLTFN314 PNKRITVEEA324 LAHPYLEQYY 334 DPTDEPVAEE344 PFTFAMELDD354 LPKERLKELI364 FQETARFQPG374 |
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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 .6H3 or .6H32 or .6H33 or :36H3;style chemicals stick;color identity;select .A:48 or .A:49 or .A:50 or .A:56 or .A:69 or .A:71 or .A:101 or .A:122 or .A:123 or .A:124 or .A:125 or .A:126 or .A:127 or .A:128 or .A:131 or .A:170 or .A:171 or .A:173 or .A:183 or .A:184; 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 | A unique inhibitor binding site in ERK1/2 is associated with slow binding kinetics. Nat Chem Biol. 2014 Oct;10(10):853-60. | ||||
| REF 2 | Crystal structure of human mono-phosphorylated ERK1 at Tyr204. Biochem Biophys Res Commun. 2008 Dec 26;377(4):1123-7. | ||||
| REF 3 | Leveraging Compound Promiscuity to Identify Targetable Cysteines within the Kinome. Cell Chem Biol. 2019 Jun 20;26(6):818-829.e9. | ||||
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