Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T58970 | Target Info | |||
| Target Name | Extracellular signal-regulated kinase 2 (ERK2) | ||||
| Synonyms | PRKM2; PRKM1; P42-MAPK; P42 Mitogen-activated protein kinase; Mitogen-activated protein kinase 2; Mitogen-activated protein kinase 1; MAPK 2; MAPK 1; MAP kinase isoform p42; MAP kinase 2; MAP kinase 1; ERT1; ERK-2 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | MAPK1 | ||||
| Biochemical Class | Kinase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Phosphonothreonine | Ligand Info | |||
| Canonical SMILES | CC(C(C(=O)O)N)OP(=O)(O)O | ||||
| InChI | 1S/C4H10NO6P/c1-2(3(5)4(6)7)11-12(8,9)10/h2-3H,5H2,1H3,(H,6,7)(H2,8,9,10)/t2-,3+/m1/s1 | ||||
| InChIKey | USRGIUJOYOXOQJ-GBXIJSLDSA-N | ||||
| PubChem Compound ID | 3246323 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5V60 Phospho-ERK2 bound to AMP-PCP | ||||||
| Method | X-ray diffraction | Resolution | 2.18 Å | Mutation | No | [1] |
| PDB Sequence |
GPEMVRGQVF
19 DVGPRYTNLS29 YIGEGAYGMV39 CSAYDNVNKV49 RVAIKKISPF59 EHQTYCQRTL 69 REIKILLRFR79 HENIIGINDI89 IRAPTIEQMK99 DVYIVQDLME109 TDLYKLLKTQ 119 HLSNDHICYF129 LYQILRGLKY139 IHSANVLHRD149 LKPSNLLLNT159 TCDLKICDFG 169 LARVADPDHD179 HTGFLEVATR191 WYRAPEIMLN201 SKGYTKSIDI211 WSVGCILAEM 221 LSNRPIFPGK231 HYLDQLNHIL241 GILGSPSQED251 LNCIINLKAR261 NYLLSLPHKN 271 KVPWNRLFPN281 ADSKALDLLD291 KMLTFNPHKR301 IEVEQALAHP311 YLEQYYDPSD 321 EPIAEAPFKF331 DMELDDLPKE341 KLKELIFEET351 ARFQPGY
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| PDB ID: 5V61 Phospho-ERK2 bound to bivalent inhibitor SBP2 | ||||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | No | [1] |
| PDB Sequence |
GPEMVRGQVF
19 DVGPRYTNLS29 YIGEGAYGMV39 CSAYDNVNKV49 RVAIKKISPF59 EHQTYCQRTL 69 REIKILLRFR79 HENIIGINDI89 IRAPTIEQMK99 DVYIVQDLME109 TDLYKLLKTQ 119 HLSNDHICYF129 LYQILRGLKY139 IHSANVLHRD149 LKPSNLLLNT159 TCDLKICDFG 169 LARVADPDHD179 HTGFLEVATR191 WYRAPEIMLN201 SKGYTKSIDI211 WSVGCILAEM 221 LSNRPIFPGK231 HYLDQLNHIL241 GILGSPSQED251 LNCIINLKAR261 NYLLSLPHKN 271 KVPWNRLFPN281 ADSKALDLLD291 KMLTFNPHKR301 IEVEQALAHP311 YLEQYYDPSD 321 EPIAEAPFKF331 DMELDDLPKE341 KLKELIFEET351 ARFQPGYR
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| PDB ID: 7OPM Phosphorylated ERK2 in complex with ORF45 | ||||||
| Method | X-ray diffraction | Resolution | 2.45 Å | Mutation | No | [2] |
| PDB Sequence |
ASMAAAAAAG
8 AGPEMVRGQV18 FDVGPRYTNL28 SYIGEGAYGM38 VCSAYDNVNK48 VRVAIKKISP 58 FEHQTYCQRT68 LREIKILLRF78 RHENIIGIND88 IIRAPTIEQM98 KDVYIVQDLM 108 ETDLYKLLKT118 QHLSNDHICY128 FLYQILRGLK138 YIHSANVLHR148 DLKPSNLLLN 158 TTCDLKICDF168 GLARVADPDH178 DHTGFLEVAT190 RWYRAPEIML200 NSKGYTKSID 210 IWSVGCILAE220 MLSNRPIFPG230 KHYLDQLNHI240 LGILGSPSQE250 DLNCIINLKA 260 RNYLLSLPHK270 NKVPWNRLFP280 NADSKALDLL290 DKMLTFNPHK300 RIEVEQALAH 310 PYLEQYYDPS320 DEPIAEAPFK330 FDMELDDLPK340 EKLKELIFEE350 TARFQPGYRS 360
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| PDB ID: 6OPH phosphorylated ERK2 with GDC-0994 | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [3] |
| PDB Sequence |
PEMVRGQVFD
18 VGPRYTNLSY28 IGEGAYGMVC38 SAYDNVNKVR48 VAIKKISPFE58 HQTYCQRTLR 68 EIKILLRFRH78 ENIIGINDII88 RAPTIEQMKD98 VYIVQDLMET108 DLYKLLKTQH 118 LSNDHICYFL128 YQILRGLKYI138 HSANVLHRDL148 KPSNLLLNTT158 CDLKICDFGL 168 ARVADPDHDH178 TGFLEVATRW190 YRAPEIMLNS200 KGYTKSIDIW210 SVGCILAEML 220 SNRPIFPGKH230 YLDQLNHILG240 ILGSPSQEDL250 NCIINLKARN260 YLLSLPHKNK 270 VPWNRLFPNA280 DSKALDLLDK290 MLTFNPHKRI300 EVEQALAHPY310 LEQYYDPSDE 320 PIAEAPFKFD330 MELDDLPKEK340 LKELIFEETA350 RFQPGY
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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:64 or .A:68 or .A:146 or .A:170 or .A:181 or .A:182 or .A:184 or .A:186 or .A:200 or .A:203; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 6OPG phosphorylated ERK2 with AMP-PNP | ||||||
| Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [3] |
| PDB Sequence |
GPEMVRGQVF
17 DVGPRYTNLS27 YIGEGAYGMV37 CSAYDNVNKV47 RVAIKKISPF57 EHQTYCQRTL 67 REIKILLRFR77 HENIIGINDI87 IRAPTIEQMK97 DVYIVQDLME107 TDLYKLLKTQ 117 HLSNDHICYF127 LYQILRGLKY137 IHSANVLHRD147 LKPSNLLLNT157 TCDLKICDFG 167 LARVADPDHD177 HTGFLEVATR189 WYRAPEIMLN199 SKGYTKSIDI209 WSVGCILAEM 219 LSNRPIFPGK229 HYLDQLNHIL239 GILGSPSQED249 LNCIINLKAR259 NYLLSLPHKN 269 KVPWNRLFPN279 ADSKALDLLD289 KMLTFNPHKR299 IEVEQALAHP309 YLEQYYDPSD 319 EPIAEAPFKF329 DMELDDLPKE339 KLKELIFEET349 ARFQPGY
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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:64 or .A:68 or .A:146 or .A:170 or .A:181 or .A:182 or .A:184 or .A:186 or .A:200 or .A:203; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 5V62 Phospho-ERK2 bound to bivalent inhibitor SBP3 | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | No | [1] |
| PDB Sequence |
GPEMVRGQVF
19 DVGPRYTNLS29 YIGEGAYGMV39 CSAYDNVNKV49 RVAIKKISPF59 EHQTYCQRTL 69 REIKILLRFR79 HENIIGINDI89 IRAPTIEQMK99 DVYIVQDLME109 TDLYKLLKTQ 119 HLSNDHICYF129 LYQILRGLKY139 IHSANVLHRD149 LKPSNLLLNT159 TCDLKICDFG 169 LARVADPDHD179 HTGFLEVATR191 WYRAPEIMLN201 SKGYTKSIDI211 WSVGCILAEM 221 LSNRPIFPGK231 HYLDQLNHIL241 GILGSPSQED251 LNCIINLKAR261 NYLLSLPHKN 271 KVPWNRLFPN281 ADSKALDLLD291 KMLTFNPHKR301 IEVEQALAHP311 YLEQYYDPSD 321 EPIAEAPFKF331 DMELDDLPKE341 KLKELIFEET351 ARFQPGYRS
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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:66 or .A:70 or .A:148 or .A:172 or .A:183 or .A:184 or .A:186 or .A:188 or .A:202 or .A:205; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structure-Guided Strategy for the Development of Potent Bivalent ERK Inhibitors. ACS Med Chem Lett. 2017 Jun 12;8(7):726-731. | ||||
| REF 2 | A non-catalytic herpesviral protein reconfigures ERK-RSK signaling by targeting kinase docking systems in the host. Nat Commun. 2022 Jan 25;13(1):472. | ||||
| REF 3 | Activation loop dynamics are controlled by conformation-selective inhibitors of ERK2. Proc Natl Acad Sci U S A. 2019 Jul 30;116(31):15463-15468. | ||||
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