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 T87675 Target Info
Target Name Aurora kinase A (AURKA)
Synonyms hARK1; Serine/threonine-protein kinase aurora-A; Serine/threonine-protein kinase 6; Serine/threonine-protein kinase 15; Serine/threonine kinase 15; STK6; STK15; IAK1; Breast tumor-amplified kinase; BTAK; Aurora/IPL1-related kinase 1; Aurora-related kinase 1; Aurora-A; Aurora 2; AYK1; AURA; ARK1; ARK-1; AIRK1; AIK
Target Type Clinical trial Target
Gene Name AURKA
Biochemical Class Kinase
UniProt ID
AURKA_HUMAN
Ligand General Information  Top
Ligand Name Adenosine triphosphate Ligand Info
Canonical SMILES C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
InChI 1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKey ZKHQWZAMYRWXGA-KQYNXXCUSA-N
PubChem Compound ID 5957
Drug Binding Sites of Target  Top
PDB ID: 1OL6      Structure of unphosphorylated D274N mutant of Aurora-A
Method X-ray diffraction Resolution 3.00 Å Mutation Yes [1]
PDB Sequence
WALEDFEIGR
137
PLGKKFGNVY
148
LAREKQSKFI
158
LALKVLFKAQ
168
LEKAEHQLRR
180

EVEIQSHLRH
190
PNILRLYGYF
200
HDATRVYLIL
210
EYAPLGTVYR
220
ELQKLSKFDE
230

QRTATYITEL
240
ANALSYCHSK
250
RVIHRDIKPE
260
NLLLGSAGEL
270
KIANFGWSVH
280

TLDYLPPEMI
301
EGMHDEKVDL
312
WSLGVLCYEF
322
LVGKPPFEAN
332
TYQETYKRIS
342

RVEFTFPDFV
352
TEGARDLISR
362
LLKHNPSQRP
372
MLREVLEHPW
382
ITANSS
Residue
Distance (Å)
LEU139
3.607
GLY140
3.249
LYS141
3.434
LYS143
2.464
PHE144
4.318
GLY145
3.261
VAL147
3.398
ALA160
4.002
LYS162
2.711
LEU164
4.039
GLU181
4.262
Residue
Distance (Å)
LEU194
3.135
LEU210
3.975
GLU211
2.861
TYR212
4.230
ALA213
3.307
THR217
3.648
GLU260
4.842
ASN261
4.965
LEU263
3.579
ASN274
3.106
PDB ID: 5DRD      Aurora A Kinase in Complex with ATP in Space Group P6122
Method X-ray diffraction Resolution 2.13 Å Mutation Yes [2]
PDB Sequence
QWALEDFEIG
136
RPLGKGKFGN
146
VYLAREKQSK
156
FILALKVLFK
166
AQLEKAGVEH
176

QLRREVEIQS
186
HLRHPNILRL
196
YGYFHDATRV
206
YLILEYAPLG
216
TVYRELQKLS
226

KFDEQRTATY
236
ITELANALSY
246
CHSKRVIHRD
256
IKPENLLLGS
266
AGELKIADFG
276

WSVHAPSSCG
291
TLDYLPPEMI
301
EGRMHDEKVD
311
LWSLGVLCYE
321
FLVGKPPFEA
331

NTYQETYKRI
341
SRVEFTFPDF
351
VTEGARDLIS
361
RLLKHNPSQR
371
PMLREVLEHP
381

WITANSSKP
Residue
Distance (Å)
LEU139
3.738
GLY140
3.306
LYS141
3.822
GLY142
3.180
LYS143
3.279
PHE144
3.138
GLY145
2.906
VAL147
3.600
ALA160
3.609
LYS162
2.809
GLN177
4.996
GLU181
2.555
LEU194
3.594
Residue
Distance (Å)
LEU210
4.111
GLU211
2.609
TYR212
3.951
ALA213
3.228
THR217
3.421
ASP256
4.451
GLU260
2.450
ASN261
2.810
LEU263
3.584
ASP274
2.351
GLY276
4.214
TRP277
4.650
PDB ID: 5DT3      Aurora A Kinase in Complex with ATP in Space Group P6122
Method X-ray diffraction Resolution 2.33 Å Mutation No [2]
PDB Sequence
QWALEDFEIG
136
RPLGKGKFGN
146
VYLAREKQSK
156
FILALKVLFK
166
AQLEKAGVEH
176

QLRREVEIQS
186
HLRHPNILRL
196
YGYFHDATRV
206
YLILEYAPLG
216
TVYRELQKLS
226

KFDEQRTATY
236
ITELANALSY
246
CHSKRVIHRD
256
IKPENLLLGS
266
AGELKIADFG
276

WSVHAPSSRR
286
TLCGTLDYLP
297
PEMIEGRMHD
307
EKVDLWSLGV
317
LCYEFLVGKP
327

PFEANTYQET
337
YKRISRVEFT
347
FPDFVTEGAR
357
DLISRLLKHN
367
PSQRPMLREV
377

LEHPWITANS
387
SKP
Residue
Distance (Å)
LEU139
3.769
GLY140
3.456
LYS141
3.524
GLY142
2.987
LYS143
3.130
PHE144
3.868
GLY145
4.757
VAL147
3.635
ALA160
3.561
LYS162
2.842
GLU181
2.782
LEU194
3.644
Residue
Distance (Å)
LEU210
4.058
GLU211
2.709
TYR212
4.053
ALA213
3.222
THR217
3.368
ASP256
4.178
GLU260
2.598
ASN261
3.073
LEU263
3.600
ASP274
2.682
GLY276
3.477
TRP277
4.504
PDB ID: 5DR2      Aurora A Kinase in Complex with AA30 and ATP in Space Group P6122
Method X-ray diffraction Resolution 2.46 Å Mutation Yes [2]
PDB Sequence
QWALEDFEIG
136
RPLGKGKFGN
146
VYLAREKQSK
156
FILALKVLFK
166
AQLEKAGVEH
176

QLRREVEIQS
186
HLRHPNILRL
196
YGYFHDATRV
206
YLILEYAPLG
216
TVYRELQKLS
226

KFDEQRTATY
236
ITELANALSY
246
CHSKRVIHRD
256
IKPENLLLGS
266
AGELKIADFG
276

WSVHAPSSRR
286
ATLCGTLDYL
296
PPEMIEGRMH
306
DEKVDLWSLG
316
VLCYEFLVGK
326

PPFEANTYQE
336
TYKRISRVEF
346
TFPDFVTEGA
356
RDLISRLLKH
366
NPSQRPMLRE
376

VLEHPWITAN
386
SSKP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:144 or .A:145 or .A:147 or .A:160 or .A:162 or .A:181 or .A:194 or .A:210 or .A:211 or .A:212 or .A:213 or .A:217 or .A:256 or .A:260 or .A:261 or .A:263 or .A:274 or .A:275 or .A:276 or .A:277; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU139
3.814
GLY140
3.527
LYS141
3.775
GLY142
3.121
LYS143
3.191
PHE144
3.687
GLY145
4.720
VAL147
3.256
ALA160
3.563
LYS162
2.903
GLU181
3.042
LEU194
3.399
LEU210
4.307
Residue
Distance (Å)
GLU211
2.715
TYR212
3.867
ALA213
3.128
THR217
3.302
ASP256
4.078
GLU260
2.770
ASN261
2.985
LEU263
3.495
ASP274
2.258
PHE275
4.804
GLY276
3.534
TRP277
4.908
PDB ID: 5DT4      Aurora A Kinase in Complex with AA35 and ATP in Space Group P6122
Method X-ray diffraction Resolution 2.86 Å Mutation No [2]
PDB Sequence
QWALEDFEIG
136
RPLGKGKFGN
146
VYLAREKQSK
156
FILALKVLFK
166
AQLEKAGVEH
176

QLRREVEIQS
186
HLRHPNILRL
196
YGYFHDATRV
206
YLILEYAPLG
216
TVYRELQKLS
226

KFDEQRTATY
236
ITELANALSY
246
CHSKRVIHRD
256
IKPENLLLGS
266
AGELKIADFG
276

WSVHAPSSCG
291
TLDYLPPEMI
301
EGRMHDEKVD
311
LWSLGVLCYE
321
FLVGKPPFEA
331

NTYQETYKRI
341
SRVEFTFPDF
351
VTEGARDLIS
361
RLLKHNPSQR
371
PMLREVLEHP
381

WITANSSKP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:144 or .A:145 or .A:147 or .A:160 or .A:162 or .A:181 or .A:194 or .A:210 or .A:211 or .A:212 or .A:213 or .A:217 or .A:256 or .A:260 or .A:261 or .A:263 or .A:274 or .A:276 or .A:277; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU139
3.593
GLY140
3.283
LYS141
3.663
GLY142
3.164
LYS143
2.817
PHE144
3.628
GLY145
4.718
VAL147
3.399
ALA160
3.327
LYS162
2.893
GLU181
3.163
LEU194
3.696
Residue
Distance (Å)
LEU210
3.997
GLU211
2.680
TYR212
3.801
ALA213
3.166
THR217
2.754
ASP256
3.606
GLU260
3.559
ASN261
2.966
LEU263
3.609
ASP274
2.362
GLY276
3.650
TRP277
4.602
PDB ID: 5DOS      Aurora A Kinase in Complex with AA35 and ATP in Space Group P6122
Method X-ray diffraction Resolution 2.98 Å Mutation Yes [2]
PDB Sequence
QWALEDFEIG
136
RPLGKGKFGN
146
VYLAREKQSK
156
FILALKVLFK
166
AQLEKAGVEH
176

QLRREVEIQS
186
HLRHPNILRL
196
YGYFHDATRV
206
YLILEYAPLG
216
TVYRELQKLS
226

KFDEQRTATY
236
ITELANALSY
246
CHSKRVIHRD
256
IKPENLLLGS
266
AGELKIADFG
276

WSVHAPSSCG
291
TLDYLPPEMI
301
EGRMHDEKVD
311
LWSLGVLCYE
321
FLVGKPPFEA
331

NTYQETYKRI
341
SRVEFTFPDF
351
VTEGARDLIS
361
RLLKHNPSQR
371
PMLREVLEHP
381

WITANSSKP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:144 or .A:145 or .A:147 or .A:160 or .A:162 or .A:181 or .A:194 or .A:210 or .A:211 or .A:212 or .A:213 or .A:217 or .A:256 or .A:260 or .A:261 or .A:263 or .A:274 or .A:276 or .A:277; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU139
3.726
GLY140
3.271
LYS141
3.696
GLY142
3.114
LYS143
3.005
PHE144
3.744
GLY145
4.956
VAL147
3.378
ALA160
3.423
LYS162
3.001
GLU181
2.965
LEU194
3.645
Residue
Distance (Å)
LEU210
4.026
GLU211
2.807
TYR212
3.732
ALA213
3.015
THR217
2.800
ASP256
3.930
GLU260
3.762
ASN261
3.153
LEU263
3.653
ASP274
2.284
GLY276
3.811
TRP277
4.837
PDB ID: 5DNR      Aurora A Kinase in complex with ATP in space group P41212
Method X-ray diffraction Resolution 1.95 Å Mutation No [2]
PDB Sequence
RQWALEDFEI
135
GRPLGKGKFG
145
NVYLAREKQS
155
KFILALKVLF
165
KAQLEKAGVE
175

HQLRREVEIQ
185
SHLRHPNILR
195
LYGYFHDATR
205
VYLILEYAPL
215
GTVYRELQKL
225

SKFDEQRTAT
235
YITELANALS
245
YCHSKRVIHR
255
DIKPENLLLG
265
SAGELKIADF
275

GWSVHAPSSR
285
RTLCGTLDYL
296
PPEMIEGRMH
306
DEKVDLWSLG
316
VLCYEFLVGK
326

PPFEANTYQE
336
TYKRISRVEF
346
TFPDFVTEGA
356
RDLISRLLKH
366
NPSQRPMLRE
376

VLEHPWITAN
386
SSKP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:144 or .A:145 or .A:147 or .A:160 or .A:162 or .A:181 or .A:194 or .A:210 or .A:211 or .A:212 or .A:213 or .A:217 or .A:256 or .A:260 or .A:261 or .A:263 or .A:274 or .A:276; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU139
3.824
GLY140
3.391
LYS141
3.704
GLY142
3.251
LYS143
3.309
PHE144
3.798
GLY145
3.132
VAL147
3.575
ALA160
3.487
LYS162
2.678
GLU181
3.314
LEU194
3.622
Residue
Distance (Å)
LEU210
3.896
GLU211
2.637
TYR212
3.917
ALA213
3.168
THR217
2.675
ASP256
4.195
GLU260
3.632
ASN261
2.904
LEU263
3.512
ASP274
2.317
GLY276
3.573
PDB ID: 5DN3      Aurora A in complex with ATP and AA35.
Method X-ray diffraction Resolution 2.05 Å Mutation No [2]
PDB Sequence
KRQWALEDFE
134
IGRPLGKGKF
144
GNVYLAREKQ
154
SKFILALKVL
164
FKAQLEKAGV
174

EHQLRREVEI
184
QSHLRHPNIL
194
RLYGYFHDAT
204
RVYLILEYAP
214
LGTVYRELQK
224

LSKFDEQRTA
234
TYITELANAL
244
SYCHSKRVIH
254
RDIKPENLLL
264
GSAGELKIAD
274

FGWSVHAPSS
284
RRTLCGTLDY
295
LPPEMIEGRM
305
HDEKVDLWSL
315
GVLCYEFLVG
325

KPPFEANTYQ
335
ETYKRISRVE
345
FTFPDFVTEG
355
ARDLISRLLK
365
HNPSQRPMLR
375

EVLEHPWITA
385
NSSK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:144 or .A:145 or .A:147 or .A:160 or .A:162 or .A:181 or .A:194 or .A:210 or .A:211 or .A:212 or .A:213 or .A:217 or .A:256 or .A:260 or .A:261 or .A:263 or .A:274 or .A:276 or .A:277; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU139
3.810
GLY140
3.511
LYS141
3.722
GLY142
2.985
LYS143
3.186
PHE144
3.612
GLY145
3.022
VAL147
3.531
ALA160
3.534
LYS162
2.770
GLU181
3.057
LEU194
3.606
Residue
Distance (Å)
LEU210
4.069
GLU211
2.782
TYR212
4.049
ALA213
3.125
THR217
3.301
ASP256
4.068
GLU260
2.705
ASN261
3.055
LEU263
3.434
ASP274
2.424
GLY276
3.503
TRP277
4.880
PDB ID: 5OBJ      Aurora A kinase in complex with 2-(3-fluorophenyl)quinoline-4-carboxylic acid and ATP
Method X-ray diffraction Resolution 2.90 Å Mutation No [3]
PDB Sequence
QWALEDFEIG
136
RPLGKGKFGN
146
VYLAREKQSK
156
FILALKVLFK
166
AQLEKAGVEH
176

QLRREVEIQS
186
HLRHPNILRL
196
YGYFHDATRV
206
YLILEYAPLG
216
TVYRELQKLS
226

KFDEQRTATY
236
ITELANALSY
246
CHSKRVIHRD
256
IKPENLLLGS
266
AGELKIADFG
276

WSVHAPSSRC
290
GTLDYLPPEM
300
IEGRMHDEKV
310
DLWSLGVLCY
320
EFLVGKPPFE
330

ANTYQETYKR
340
ISRVEFTFPD
350
FVTEGARDLI
360
SRLLKHNPSQ
370
RPMLREVLEH
380

PWITANSSKP
390
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:144 or .A:147 or .A:160 or .A:162 or .A:164 or .A:181 or .A:194 or .A:210 or .A:211 or .A:212 or .A:213 or .A:217 or .A:260 or .A:261 or .A:263 or .A:274 or .A:276 or .A:277; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU139
3.842
GLY140
3.604
LYS141
3.458
GLY142
3.111
LYS143
2.655
PHE144
3.232
VAL147
3.527
ALA160
3.323
LYS162
3.070
LEU164
3.827
GLU181
3.753
LEU194
3.819
Residue
Distance (Å)
LEU210
4.528
GLU211
2.899
TYR212
4.202
ALA213
3.614
THR217
3.220
GLU260
3.279
ASN261
3.348
LEU263
3.576
ASP274
2.810
GLY276
3.968
TRP277
4.466
References  Top
REF 1 Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol Cell. 2003 Oct;12(4):851-62.
REF 2 Allosteric modulation of AURKA kinase activity by a small-molecule inhibitor of its protein-protein interaction with TPX2. Sci Rep. 2016 Jun 24;6:28528.
REF 3 Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase-TPX2 protein-protein interaction. Chem Commun (Camb). 2017 Aug 17;53(67):9372-9375.

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