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 | AMP-PNP | Ligand Info | |||
| Canonical SMILES | C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N | ||||
| InChI | 1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1 | ||||
| InChIKey | PVKSNHVPLWYQGJ-KQYNXXCUSA-N | ||||
| PubChem Compound ID | 33113 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 2Y9Q Crystal structure of human ERK2 complexed with a MAPK docking peptide | ||||||
| Method | X-ray diffraction | Resolution | 1.55 Å | Mutation | Yes | [1] |
| PDB Sequence |
AGPEMVRGQV
18 FDVGPRYTNL28 SYIGEGAYGM38 VCSAYDNVNK48 VRVAIKKISP58 FEHQTYCQRT 68 LREIKILLRF78 RHENIIGIND88 IIRAPTIEQM98 KDVYIVQDLM108 ETDLYKLLKT 118 QHLSNDHICY128 FLYQILRGLK138 YIHSANVLHR148 DLKPSNLLLN158 TTCDLKICDF 168 GLARVADPDH178 DHTGFLTEYV188 ATRWYRAPEI198 MLNSKGYTKS208 IDIWSVGCIL 218 AEMLSNRPIF228 PGKHYLDQLN238 HILGILGSPS248 QEDLNCIINL258 KARNYLLSLP 268 HKNKVPWNRL278 FPNADSKALD288 LLDKMLTFNP298 HKRIEVEQAL308 AHPYLEQYYD 318 PSDEPIAEAP328 FKFDMELDDL338 PKEKLKELIF348 EETARFQPGY358 |
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|
|
ILE31
4.244
GLY32
4.883
GLU33
4.285
GLY34
3.043
ALA35
2.775
TYR36
2.866
GLY37
2.763
VAL39
3.362
ALA52
3.483
LYS54
2.773
ILE56
4.808
ARG67
3.444
GLU71
4.486
ILE84
4.002
GLN105
3.018
|
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| PDB ID: 4FMQ Crystal structure of human ERK2 complexed with a MAPK docking peptide | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [1] |
| PDB Sequence |
AGPEMVRGQV
18 FDVGPRYTNL28 SYIGEGAYGM38 VCSAYDNVNK48 VRVAIKKISP58 FEHQTYCQRT 68 LREIKILLRF78 RHENIIGIND88 IIRAPTIEQM98 KDVYIVQDLM108 ETDLYKLLKT 118 QHLSNDHICY128 FLYQILRGLK138 YIHSANVLHR148 DLKPSNLLLN158 TTCDLKICDF 168 GLARVADPDH178 DHTGFLTEYV188 ATRWYRAPEI198 MLNSKGYTKS208 IDIWSVGCIL 218 AEMLSNRPIF228 PGKHYLDQLN238 HILGILGSPS248 QEDLNCIINL258 KARNYLLSLP 268 HKNKVPWNRL278 FPNADSKALD288 LLDKMLTFNP298 HKRIEVEQAL308 AHPYLEQYYD 318 PSDEPIAEAP328 FKFDMELDDL338 PKEKLKELIF348 EETARFQPGY358 |
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|
|
ILE31
4.012
GLY32
4.691
GLU33
4.154
GLY34
2.840
ALA35
2.758
TYR36
2.766
GLY37
2.990
VAL39
3.273
ALA52
3.449
LYS54
2.853
ARG67
3.472
GLU71
4.682
ILE84
3.945
GLN105
3.138
|
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| PDB ID: 4NIF Heterodimeric structure of ERK2 and RSK1 | ||||||
| Method | X-ray diffraction | Resolution | 2.15 Å | Mutation | No | [2] |
| PDB Sequence |
AGPEMVRGQV
18 FDVGPRYTNL28 SYIGEGAYGM38 VCSAYDNVNK48 VRVAIKKISP58 FEHQTYCQRT 68 LREIKILLRF78 RHENIIGIND88 IIRAPTIEQM98 KDVYIVQDLM108 ETDLYKLLKT 118 QHLSNDHICY128 FLYQILRGLK138 YIHSANVLHR148 DLKPSNLLLN158 TTCDLKICDF 168 GLARVADPDH178 GFLTEYVATR191 WYRAPEIMLN201 SKGYTKSIDI211 WSVGCILAEM 221 LSNRPIFPGK231 HYLDQLNHIL241 GILGSPSQED251 LNCIINLKAR261 NYLLSLPHKN 271 KVPWNRLFPN281 ADSKALDLLD291 KMLTFNPHKR301 IEVEQALAHP311 YLEQYYDPSD 321 EPIAEAPFKF331 DMELDDLPKE341 KLKELIFEET351 ARFQPGYRS
|
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|
|
ILE31
3.851
GLY32
4.128
GLU33
3.776
GLY34
3.164
ALA35
2.824
TYR36
2.903
GLY37
2.858
VAL39
3.263
ALA52
3.427
LYS54
2.761
ILE56
4.636
ARG67
3.309
GLU71
4.457
ILE84
4.103
|
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| PDB ID: 4H3Q Crystal structure of human ERK2 complexed with a MAPK docking peptide | ||||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [3] |
| PDB Sequence |
AGPEMVRGQV
18 FDVGPRYTNL28 SYIGEGAYGM38 VCSAYDNVNK48 VRVAIKKISP58 FEHQTYCQRT 68 LREIKILLAF78 RHENIIGIND88 IIRAPTIEQM98 KDVYIVQDLM108 ETDLYKLLKT 118 QHLSNDHICY128 FLYQILRGLK138 YIHSANVLHR148 DLKPSNLLLN158 TTSDLKICDF 168 GLARVADPDH178 DHTGFLTEYV188 ATRWYRAPEI198 MLNSKGYTKS208 IDIWSVGCIL 218 AEMLSNRPIF228 PGKHYLDQLN238 HILGILGSPS248 QEDLNCGINL258 KARNYLLSLP 268 HKNKVPWNRL278 FPNADSKALD288 LLDKMLTFNP298 HKRIEVEQAL308 AHPYLAQYYD 318 PSDEPIAEAP328 FKFDMELDDL338 PKEKLKELIF348 EETARFQPGY358 RS |
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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 .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:36 or .A:37 or .A:39 or .A:52 or .A:54 or .A:67 or .A:84 or .A:105 or .A:106 or .A:107 or .A:108 or .A:109 or .A:111 or .A:114 or .A:149 or .A:151 or .A:153 or .A:154 or .A:156 or .A:166 or .A:167; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE31
4.002
GLY32
4.905
GLU33
4.415
GLY34
3.235
ALA35
2.963
TYR36
2.719
GLY37
3.425
VAL39
3.544
ALA52
3.568
LYS54
3.167
ARG67
3.870
ILE84
3.857
GLN105
3.005
|
|||||
| PDB ID: 4H3P Crystal structure of human ERK2 complexed with a MAPK docking peptide | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | Yes | [3] |
| PDB Sequence |
PEMVRGQVFD
20 VGPRYTNLSY30 IGEGAYGMVC40 SAYDNVNKVR50 VAIKKISPFE60 HQTYCQRTLR 70 EIKILLAFRH80 ENIIGINDII90 RAPTIEQMKD100 VYIVQDLMET110 DLYKLLKTQH 120 LSNDHICYFL130 YQILRGLKYI140 HSANVLHRDL150 KPSNLLLNTT160 CDLKICDFGL 170 ARVADPDHEY187 VATRWYRAPE197 IMLNSKGYTK207 SIDIWSVGCI217 LAEMLSNRPI 227 FPGKHYLDQL237 NHILGILGSP247 SQEDLNCIIN257 LKARNYLLSL267 PHKNKVPWNR 277 LFPNADSKAL287 DLLDKMLTFN297 PHKRIEVEQA307 LAHPYLAQYY317 DPSDEPIAEA 327 PFKFDMELDD337 LPKEKLKELI347 FEETARFQPG357 YR
|
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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 .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:37 or .A:39 or .A:52 or .A:54 or .A:84 or .A:105 or .A:106 or .A:107 or .A:108 or .A:110 or .A:111 or .A:114 or .A:151 or .A:153 or .A:154 or .A:156 or .A:167; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE31
3.955
GLY32
4.054
GLU33
4.047
GLY34
3.569
ALA35
4.861
GLY37
4.154
VAL39
3.452
ALA52
3.476
LYS54
4.337
ILE84
4.158
GLN105
3.398
|
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| PDB ID: 3TEI Crystal structure of human ERK2 complexed with a MAPK docking peptide | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | Yes | [1] |
| PDB Sequence |
GPEMVRGQVF
19 DVGPRYTNLS29 YIGEGAYGMV39 CSAYDNVNKV49 RVAIKKISPF59 EHQTYCQRTL 69 REIKILLAFR79 HENIIGINDI89 IRAPTIEQMK99 DVYIVQDLME109 TDLYKLLKTQ 119 HLSNDHICYF129 LYQILRGLKY139 IHSANVLHRD149 LKPSNLLLNT159 TCDLKICDFG 169 LARVADPDHE186 YVATRWYRAP196 EIMLNYTKSI209 DIWSVGCILA219 EMLSNRPIFP 229 GKHYLDQLNH239 ILGILGSPSQ249 EDLNCIINLK259 ARNYLLSLPH269 KNKVPWNRLF 279 PNADSKALDL289 LDKMLTFNPH299 KRIEVEQALA309 HPYLAQYYDP319 SDEPIAEAPF 329 KFDMELDDLP339 KEKLKELIFE349 ETARFQPGY
|
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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 .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:31 or .A:32 or .A:33 or .A:34 or .A:35 or .A:39 or .A:52 or .A:54 or .A:84 or .A:105 or .A:106 or .A:107 or .A:108 or .A:110 or .A:111 or .A:114 or .A:149 or .A:151 or .A:153 or .A:154 or .A:156 or .A:166 or .A:167; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE31
3.822
GLY32
4.292
GLU33
3.328
GLY34
3.156
ALA35
2.467
VAL39
2.996
ALA52
3.487
LYS54
3.327
ILE84
4.040
GLN105
3.233
ASP106
2.929
LEU107
3.822
|
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| PDB ID: 6OPG phosphorylated ERK2 with AMP-PNP | ||||||
| Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [4] |
| 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 .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:29 or .A:30 or .A:31 or .A:32 or .A:33 or .A:35 or .A:37 or .A:50 or .A:52 or .A:69 or .A:82 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:109 or .A:112 or .A:147 or .A:149 or .A:151 or .A:152 or .A:154 or .A:164 or .A:165; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ILE29
3.360
GLY30
4.096
GLU31
3.296
GLY32
3.379
ALA33
4.919
GLY35
4.359
VAL37
3.447
ALA50
3.524
LYS52
3.230
GLU69
4.941
ILE82
3.972
GLN103
3.308
ASP104
2.938
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove. Sci Signal. 2012 Oct 9;5(245):ra74. | ||||
| REF 2 | Structural assembly of the signaling competent ERK2-RSK1 heterodimeric protein kinase complex. Proc Natl Acad Sci U S A. 2015 Mar 3;112(9):2711-6. | ||||
| REF 3 | Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase. Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):486-9. | ||||
| REF 4 | 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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