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 T59537 Target Info
Target Name Membrane-associated kinase (PKMYT1)
Synonyms Myt1 kinase; Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase; MYT1
Target Type Literature-reported Target
Gene Name PKMYT1
Biochemical Class Kinase
UniProt ID
PMYT1_HUMAN
Ligand General Information  Top
Ligand Name Saracatinib Ligand Info
Canonical SMILES CN1CCN(CC1)CCOC2=CC3=C(C(=C2)OC4CCOCC4)C(=NC=N3)NC5=C(C=CC6=C5OCO6)Cl
InChI 1S/C27H32ClN5O5/c1-32-6-8-33(9-7-32)10-13-35-19-14-21-24(23(15-19)38-18-4-11-34-12-5-18)27(30-16-29-21)31-25-20(28)2-3-22-26(25)37-17-36-22/h2-3,14-16,18H,4-13,17H2,1H3,(H,29,30,31)
InChIKey OUKYUETWWIPKQR-UHFFFAOYSA-N
PubChem Compound ID 10302451
Drug Binding Sites of Target  Top
PDB ID: 5VD3      CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN (de-phosphorylated) IN COMPLEX WITH SARACATINIB
Method X-ray diffraction Resolution 1.80 Å Mutation No [1]
PDB Sequence
DLGTENLYFQ
-2
QPRRVSFRGE
87
ASETLQSPGY
97
DPSRPESFFQ
107
QSFQRLSRLG
117

HGSYGEVFKV
127
RSKEDGRLYA
137
VKRSMSPFRG
147
PKDRARKLAE
157
VGSHEKVGQH
167

PCCVRLEQAW
177
EEGGILYLQT
187
ELCGPSLQQH
197
CEAWGASLPE
207
AQVWGYLRDT
217

LLALAHLHSQ
227
GLVHLDVKPA
237
NIFLGPRGRC
247
KLGDFGLLVE
257
LGTAGAGEVQ
267

EGDPRYMAPE
277
LLQGSYGTAA
287
DVFSLGLTIL
297
EVACNMELPH
307
GGEGWQQLRQ
317

GYLPPEFTAG
327
LSSELRSVLV
337
MMLEPDPKLR
347
ATAEALLALP
357
VLR
Residue
Distance (Å)
SER114
3.887
LEU116
2.133
GLY117
2.158
HIS118
4.615
TYR121
3.070
VAL124
2.709
LYS126
4.013
ALA137
2.759
VAL138
2.936
LYS139
2.369
GLU157
2.693
VAL171
3.847
LEU185
2.640
GLN186
4.136
Residue
Distance (Å)
THR187
2.300
GLU188
2.568
LEU189
2.738
CYS190
2.250
GLY191
2.537
PRO192
2.320
SER193
3.152
GLN195
4.173
GLN196
2.820
ALA237
2.397
ASN238
4.029
PHE240
2.161
ASP251
2.407
PHE252
4.627
PDB ID: 5VCX      CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN (UNTREATED) IN COMPLEX WITH SARACATINIB
Method X-ray diffraction Resolution 2.70 Å Mutation No [1]
PDB Sequence
HQLQPRRVSF
84
RGEASETLQS
94
PGYDPSRPES
104
FFQQSFQRLS
114
RLGHGSYGEV
124

FKVRSKEDGR
134
LYAVKRSMSP
144
FRGPKDRARK
154
LAEVGSHEKV
164
GQHPCCVRLE
174

QAWEEGGILY
184
LQTELCGPSL
194
QQHCEAWGAS
204
LPEAQVWGYL
214
RDTLLALAHL
224

HSQGLVHLDV
234
KPANIFLGPR
244
GRCKLGDFGL
254
LVELGTAGAG
264
EVQEGDPRYM
274

APELLQGSYG
284
TAADVFSLGL
294
TILEVACNME
304
LPHGGEGWQQ
314
LRQGYLPPEF
324

TAGLSSELRS
334
VLVMMLEPDP
344
KLRATAEALL
354
ALPVLRQ
Residue
Distance (Å)
LEU116
3.335
GLY117
3.745
TYR121
3.555
VAL124
3.634
ALA137
3.248
VAL138
4.207
LYS139
3.587
GLU157
4.232
LEU185
3.542
THR187
3.526
GLU188
3.497
Residue
Distance (Å)
LEU189
3.986
CYS190
3.186
GLY191
3.631
PRO192
3.755
SER193
4.317
GLN196
3.960
ALA237
3.963
ASN238
4.617
PHE240
3.461
ASP251
3.342
References  Top
REF 1 Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors. J Med Chem. 2017 Sep 28;60(18):7863-7875.

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