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 T85435 Target Info
Target Name Insulin receptor (INSR)
Synonyms IR; CD220 antigen; CD220
Target Type Successful Target
Gene Name INSR
Biochemical Class Kinase
UniProt ID
INSR_HUMAN
Ligand General Information  Top
Ligand Name L-betagamma-meATP Ligand Info
Canonical SMILES C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(CP(=O)(O)O)O)O)O)N
InChI 1S/C11H18N5O12P3/c12-9-6-10(14-2-13-9)16(3-15-6)11-8(18)7(17)5(27-11)1-26-31(24,25)28-30(22,23)4-29(19,20)21/h2-3,5,7-8,11,17-18H,1,4H2,(H,22,23)(H,24,25)(H2,12,13,14)(H2,19,20,21)/t5-,7-,8-,11-/m1/s1
InChIKey UFZTZBNSLXELAL-IOSLPCCCSA-N
PubChem Compound ID 91532
Drug Binding Sites of Target  Top
PDB ID: 4XLV      Crystal structure of the activated insulin receptor tyrosine kinase dimer
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [1]
PDB Sequence
SASDVFPSSV
983
YVPDEWEVSR
993
EKITLLRELG
1003
QGSFGMVYEG
1013
NARDIIKGEA
1023

ETRVAVKTVN
1033
ESASLRERIE
1043
FLNEASVMKG
1053
FTCHHVVRLL
1063
GVVSKGQPTL
1073

VVMELMAHGD
1083
LKSYLRSLRP
1093
EAENNPGRPP
1103
PTLQEMIQMA
1113
AEIADGMAYL
1123

NAKKFVHRDL
1133
AARNCMVAHD
1143
FTVKIGDFGM
1153
TRDIETDRKG
1166
GKGLLPVRWM
1176

APESLKDGVF
1186
TTSSDMWSFG
1196
VVLWEITSLA
1206
EQPYQGLSNE
1216
QVLKFVMDGG
1226

YLDQPDNCPE
1236
RVTDLMRMCW
1246
QFNPNMRPTF
1256
LEIVNLLKDD
1266
LHPSFPEVSF
1276

FHSEENK
Residue
Distance (Å)
LEU1002
3.632
GLY1003
3.952
GLY1005
3.477
SER1006
4.767
PHE1007
3.797
GLY1008
4.163
VAL1010
3.587
ALA1028
3.426
LYS1030
2.763
GLU1043
3.295
GLU1047
2.894
VAL1060
3.938
MET1076
2.881
Residue
Distance (Å)
GLU1077
3.059
LEU1078
3.922
MET1079
2.886
ALA1080
4.950
GLY1082
3.756
ASP1083
2.732
ASP1132
4.577
ARG1136
3.348
ASN1137
3.193
MET1139
3.424
ASP1150
2.758
GLY1152
3.809
PDB ID: 1I44      CRYSTALLOGRAPHIC STUDIES OF AN ACTIVATION LOOP MUTANT OF THE INSULIN RECEPTOR TYROSINE KINASE
Method X-ray diffraction Resolution 2.40 Å Mutation Yes [2]
PDB Sequence
PDEWEVSREK
995
ITLLRELGQG
1005
SFGMVYEGNA
1015
RDIIKGEAET
1025
RVAVKTVNES
1035

ASLRERIEFL
1045
NEASVMKGFT
1055
CHHVVRLLGV
1065
VSKGQPTLVV
1075
MELMAHGDLK
1085

SYLRSLRPEA
1095
ENNPGRPPPT
1105
LQEMIQMAAE
1115
IADGMAYLNA
1125
KKFVHRDLAA
1135

RNCMVAHDFT
1145
VKIGDFGMTL
1171
PVRWMAPESL
1181
KDGVFTTSSD
1191
MWSFGVVLWE
1201

ITSLAEQPYQ
1211
GLSNEQVLKF
1221
VMDGGYLDQP
1231
DNCPERVTDL
1241
MRMCWQFNPK
1251

MRPTFLEIVN
1261
LLKDDLHPSF
1271
PEVSFFHSEE
1281
NK
Residue
Distance (Å)
LEU1002
3.515
GLY1003
3.967
GLN1004
3.206
GLY1005
3.552
SER1006
2.661
PHE1007
4.574
VAL1010
3.674
ALA1028
3.363
LYS1030
2.954
VAL1060
3.760
MET1076
3.991
Residue
Distance (Å)
GLU1077
2.987
LEU1078
3.773
MET1079
2.967
GLY1082
4.773
ASP1083
3.960
ASP1132
4.256
ARG1136
4.661
ASN1137
3.817
MET1139
3.672
ASP1150
3.114
MET1153
4.954
References  Top
REF 1 The insulin and IGF1 receptor kinase domains are functional dimers in the activated state. Nat Commun. 2015 Mar 11;6:6406.
REF 2 Crystallographic and solution studies of an activation loop mutant of the insulin receptor tyrosine kinase: insights into kinase mechanism. J Biol Chem. 2001 Mar 30;276(13):10049-55.

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