Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
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
MK01_HUMAN
Ligand General Information  Top
Ligand Name 5'-iodotubercidin Ligand Info
Canonical SMILES C1=C(C2=C(N=CN=C2N1C3C(C(C(O3)CO)O)O)N)I
InChI 1S/C11H13IN4O4/c12-4-1-16(10-6(4)9(13)14-3-15-10)11-8(19)7(18)5(2-17)20-11/h1,3,5,7-8,11,17-19H,2H2,(H2,13,14,15)/t5-,7-,8-,11-/m1/s1
InChIKey WHSIXKUPQCKWBY-IOSLPCCCSA-N
PubChem Compound ID 97297
Drug Binding Sites of Target  Top
PDB ID: 7W5O      Crystal structure of ERK2 with an allosteric inhibitor
Method X-ray diffraction Resolution 2.35 Å Mutation No [1]
PDB Sequence
PEMVRGQVFD
20
VGPRYTNLSY
30
IGEGAYGMVC
40
SAYDNVNKVR
50
VAIKKISPFE
60

HQTYCQRTLR
70
EIKILLRFRH
80
ENIIGINDII
90
RAPTIEQMKD
100
VYIVQDLMET
110

DLYKLLKTQH
120
LSNDICYFLY
131
QILRGLKYIH
141
SANVLHRDLK
151
PSNLLLNTTC
161

DLKICDFGLA
171
RVADPDHDHT
181
GFLTEYVATR
191
WYRAPEIMLN
201
SKGYTKSIDI
211

WSVGCILAEM
221
LSNRPIFPGK
231
HYLDQLNHIL
241
GILGSPSQED
251
LNCIINLKAR
261

NYLLSLPHKN
271
KVPWNRLFPN
281
ADSKALDLLD
291
KMLTFNPHKR
301
IEVEQALAHP
311

YLEQYYDPSD
321
EPIAEAPFKF
331
DMELDDLPKE
341
KLKELIFEET
351
ARFQPGYRS
Residue
Distance (Å)
ILE31
3.680
GLY32
3.982
GLU33
4.113
VAL39
3.519
ALA52
3.055
LYS54
4.349
ILE84
4.075
GLN105
3.299
ASP106
2.406
LEU107
3.856
Residue
Distance (Å)
MET108
2.226
GLU109
4.342
THR110
4.604
ASP111
2.078
LYS114
2.360
SER153
2.399
ASN154
3.450
LEU156
3.092
CYS166
4.160
PDB ID: 5AX3      Crystal structure of ERK2 complexed with allosteric and ATP-competitive inhibitors.
Method X-ray diffraction Resolution 2.98 Å Mutation No [2]
PDB Sequence
GPEMVRGQVF
10
DVGPRYTNLS
20
YIGEYGMVCS
32
AYDNVNKVRV
42
AIKKISPFEH
52

QTYCQRTLRE
62
IKILLRFRHE
72
NIIGINDIIR
82
APTIEQMKDV
92
YIVQDLMETD
102

LYKLLKTQHL
112
SNDHICYFLY
122
QILRGLKYIH
132
SANVLHRDLK
142
PSNLLLNTTC
152

DLKICDFGLA
162
RVAFLTEYVT
181
RWYRAPEIML
191
GYTKSIDIWS
203
VGCILAEMLS
213

NRPIFPGKHY
223
LDQLNHILGI
233
LGSPSQEDLK
249
ARNYLLSLPH
259
KNKVPWNRLF
269

PNADSKALDL
279
LDKMLTFNPH
289
KRIEVEQALA
299
HPYLEQYYDP
309
SDEPIAEAPF
319

KFDMELDDLP
329
KEKLKELIFE
339
ETARFQPGY
Residue
Distance (Å)
ILE22
3.293
GLU24
2.802
VAL30
3.927
ALA43
3.386
LYS45
4.353
ILE75
4.269
GLN96
3.771
ASP97
3.130
Residue
Distance (Å)
LEU98
3.597
MET99
2.954
THR101
4.586
ASP102
2.150
LYS105
2.543
SER144
3.297
LEU147
3.499
CYS157
4.593
References  Top
REF 1 Identification of a novel target site for ATP-independent ERK2 inhibitors. Biochem Biophys Res Commun. 2022 Feb 19;593:73-78.
REF 2 Identification of allosteric ERK2 inhibitors through in silico biased screening and competitive binding assay. Bioorg Med Chem Lett. 2016 Feb 1;26(3):955-958.

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