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 T65864 Target Info
Target Name Stress-activated protein kinase 2a (p38 alpha)
Synonyms SAPK2A; P38 mitogen activatedprotein kinase; P38 Mitogen-activatedprotein kinase alpha; Mitogen-activated protein kinase p38 alpha; Mitogen-activated protein kinase 14; MXI2; MAX-interacting protein 2; MAPK 14; MAP kinase p38alpha; MAP kinase p38 alpha; MAP kinase MXI2; MAP kinase 14; Cytokine suppressive anti-inflammatory drug-binding protein; Cytokine suppressive anti-inflammatory drug binding protein; CSPB1; CSBP2; CSBP1; CSBP; CSAID-binding protein; CSAID binding protein; CRK1
Target Type Clinical trial Target
Gene Name MAPK14
Biochemical Class Kinase
UniProt ID
MK14_HUMAN
Ligand General Information  Top
Ligand Name Doramapimod Ligand Info
Canonical SMILES CC1=CC=C(C=C1)N2C(=CC(=N2)C(C)(C)C)NC(=O)NC3=CC=C(C4=CC=CC=C43)OCCN5CCOCC5
InChI 1S/C31H37N5O3/c1-22-9-11-23(12-10-22)36-29(21-28(34-36)31(2,3)4)33-30(37)32-26-13-14-27(25-8-6-5-7-24(25)26)39-20-17-35-15-18-38-19-16-35/h5-14,21H,15-20H2,1-4H3,(H2,32,33,37)
InChIKey MVCOAUNKQVWQHZ-UHFFFAOYSA-N
PubChem Compound ID 156422
Drug Binding Sites of Target  Top
PDB ID: 5N66      Crystal Structure of p38alpha in Complex with Lipid Pocket Ligand 9j
Method X-ray diffraction Resolution 2.40 Å Mutation No [1]
PDB Sequence
PTFYRQELNK
15
TIWEVPERYQ
25
NLSPVGSGSV
38
CAAFDTKTGL
48
RVAVKKLSRP
58

FQSIIHAKRT
68
YRELRLLKHM
78
KHENVIGLLD
88
VFTPARSLEE
98
FNDVYLVTHL
108

MGADLNNIVK
118
CQKLTDDHVQ
128
FLIYQILRGL
138
KYIHSADIIH
148
RDLKPSNLAV
158

NEDCELKILD
168
FVATRWYRAP
191
EIMLNWMHYN
201
QTVDIWSVGC
211
IMAELLTGRT
221

LFPGTDHIDQ
231
LKLILRLVGT
241
PGAELLKKIS
251
SESARNYIQS
261
LTQMPKMNFA
271

NVFIGANPLA
281
VDLLEKMLVL
291
DSDKRITAAQ
301
ALAHAYFAQY
311
HDPDDEPVAD
321

PYDQSFESRD
331
LLIDEWKSLT
341
YDEVISFVPP
351
PL
Residue
Distance (Å)
VAL30
4.733
VAL38
3.774
ALA51
3.811
LYS53
3.595
ARG67
3.469
ARG70
4.392
GLU71
3.265
LEU74
3.549
LEU75
3.781
MET78
3.616
VAL83
3.905
ILE84
3.792
LEU104
3.681
Residue
Distance (Å)
VAL105
4.867
THR106
3.473
HIS107
3.292
LEU108
3.713
MET109
3.144
ILE141
4.430
HIS148
3.687
ALA157
4.137
ILE166
3.659
LEU167
3.386
ASP168
2.671
PHE169
3.545
PDB ID: 1KV2      Human p38 MAP Kinase in Complex with BIRB 796
Method X-ray diffraction Resolution 2.80 Å Mutation No [2]
PDB Sequence
RPTFYRQELN
14
KTIWEVPERY
24
QNLSPVGSGA
34
YGSVCAAFDT
44
KTGLRVAVKK
54

LSRPFQSIIH
64
AKRTYRELRL
74
LKHMKHENVI
84
GLLDVFTPAR
94
SLEEFNDVYL
104

VTHLMGADLN
114
TDDHVQFLIY
132
QILRGLKYIH
142
SADIIHRDLK
152
PSNLAVNEDC
162

ELKILDFTRW
187
YRAPEIMLNW
197
MHYNQTVDIW
207
SVGCIMAELL
217
TGRTLFPGTD
227

HIDQLKLILR
237
LVGTPGAELL
247
KKISSESARN
257
YIQSLTQMPK
267
MNFANVFIGA
277

NPLAVDLLEK
287
MLVLDSDKRI
297
TAAQALAHAY
307
FAQYHDPDDE
317
PVADPYDQSF
327

ESRDLLIDEW
337
KSLTYDEVIS
347
FVPPP
Residue
Distance (Å)
VAL30
4.780
VAL38
3.582
ALA51
3.976
VAL52
4.735
LYS53
3.814
ARG67
3.201
ARG70
4.225
GLU71
2.977
LEU74
3.727
LEU75
3.608
MET78
3.870
VAL83
4.036
ILE84
3.713
LEU104
3.552
VAL105
4.208
Residue
Distance (Å)
THR106
3.595
HIS107
4.112
LEU108
3.102
MET109
2.900
GLY110
3.233
ALA111
4.671
ILE141
4.939
ILE146
4.645
HIS148
3.691
ALA157
4.309
ILE166
3.836
LEU167
3.148
ASP168
2.890
PHE169
3.126
References  Top
REF 1 Structure-based design, synthesis and crystallization of 2-arylquinazolines as lipid pocket ligands of p38Alpha MAPK. PLoS One. 2017 Sep 11;12(9):e0184627.
REF 2 Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nat Struct Biol. 2002 Apr;9(4):268-72.

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