Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T92966 | Target Info | |||
| Target Name | Hepatocellular carcinoma-associated antigen 90 (TPX2) | ||||
| Synonyms | Restricted expression proliferation-associated protein 100; Protein fls353; Hepatocellular carcinoma-associated antigen 519; HCA519; Differentially expressed in cancerous and non-cancerous lung cells 2; DIL2; DIL-2; C20orf2; C20orf1 | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | TPX2 | ||||
| Biochemical Class | TPX2 family | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | AMP-PNP | Ligand Info | |||
| Canonical SMILES | C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N | ||||
| InChI | 1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1 | ||||
| InChIKey | PVKSNHVPLWYQGJ-KQYNXXCUSA-N | ||||
| PubChem Compound ID | 33113 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6VPL TPX2 residues 7-20 fused to Aurora A residues 116-389 with C290 disulfide bonded to compound 7-80, and in complex with AMP-PNP | ||||||
| Method | X-ray diffraction | Resolution | 1.86 Å | Mutation | No | [1] |
| PDB Sequence |
MSYSYDAPSD
15 FINFSSKRQW128 ALEDFEIGRP138 LGKGKFGNVY148 LAREKQSKFI158 LALKVLFKAQ 168 LEKAGVEHQL178 RREVEIQSHL188 RHPNILRLYG198 YFHDATRVYL208 ILEYAPLGTV 218 YRELQKLSKF228 DEQRTATYIT238 ELANALSYCH248 SKRVIHRDIK258 PENLLLGSAG 268 ELKIADFGWS278 VHAPTLCGTL293 DYLPPEMIEG303 RMHDEKVDLW313 SLGVLCYEFL 323 VGKPPFEANT333 YQETYKRISR343 VEFTFPDFVT353 EGARDLISRL363 LKHNPSQRPM 373 LREVLEHPWI383 TANSSK
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| PDB ID: 6VPI TPX2 residues 7-20 fused to Aurora A residues 116-389 C247V + D256N + C319V triple mutant disulfide homodimer in complex with AMP-PNP | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
SYSYDAPSDF
16 INFSRQWALE131 DFEIGRPLGK141 GKFGNVYLAR151 EKQSKFILAL161 KVLFKAQLEK 171 AGVEHQLRRE181 VEIQSHLRHP191 NILRLYGYFH201 DATRVYLILE211 YAPLGTVYRE 221 LQKLSKFDEQ231 RTATYITELA241 NALSYVHSKR251 VIHRNIKPEN261 LLLGSAGELK 271 IADFGWSVHA281 PSSRRTTLCG291 TLDYLPPEMI301 EGRMHDEKVD311 LWSLGVLVYE 321 FLVGKPPFEA331 NTYQETYKRI341 SRVEFTFPDF351 VTEGARDLIS361 RLLKHNPSQR 371 PMLREVLEHP381 WITANSSK
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| PDB ID: 6VPJ TPX2 residues 7-20 fused to Aurora A residues 116-389 C247V + C319V double mutant dephosphorylated, and in complex with AMP-PNP | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [1] |
| PDB Sequence |
MSYSYDAPSD
15 FINFSSKKRQ127 WALEDFEIGR137 PLGKGKFGNV147 YLAREKQSKF157 ILALKVLFKA 167 QLEKAGVEHQ177 LRREVEIQSH187 LRHPNILRLY197 GYFHDATRVY207 LILEYAPLGT 217 VYRELQKLSK227 FDEQRTATYI237 TELANALSYV247 HSKRVIHRDI257 KPENLLLGSA 267 GELKIADFGW277 SVHAPSTTLC290 GTLDYLPPEM300 IEGRMHDEKV310 DLWSLGVLVY 320 EFLVGKPPFE330 ANTYQETYKR340 ISRVEFTFPD350 FVTEGARDLI360 SRLLKHNPSQ 370 RPMLREVLEH380 PWITANSSK
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LEU139
3.797
GLY140
3.276
LYS141
3.770
GLY142
3.139
LYS143
3.353
PHE144
2.748
GLY145
2.790
ASN146
4.826
VAL147
3.755
ALA160
3.672
LYS162
2.577
LEU164
4.719
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| PDB ID: 6VPH TPX2 residues 7-20 fused to Aurora A residues 116-389 modified with cacodylate and in complex with AMP-PNP | ||||||
| Method | X-ray diffraction | Resolution | 2.14 Å | Mutation | No | [1] |
| PDB Sequence |
HMSYSYDAPS
14 DFINFSSSKK125 RQWALEDFEI135 GRPLGKGKFG145 NVYLAREKQS155 KFILALKVLF 165 KAQLEKAGVE175 HQLRREVEIQ185 SHLRHPNILR195 LYGYFHDATR205 VYLILEYAPL 215 GTVYRELQKL225 SKFDEQRTAT235 YITELANALS245 YHSKRVIHRD256 IKPENLLLGS 266 AGELKIADFG276 WSVHAPSSRR286 LGTLDYLPPE299 MIEGRMHDEK309 VDLWSLGVLC 319 YEFLVGKPPF329 EANTYQETYK339 RISRVEFTFP349 DFVTEGARDL359 ISRLLKHNPS 369 QRPMLREVLE379 HPWITANSSK389
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ANP or .ANP2 or .ANP3 or :3ANP;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:164 or .A:194 or .A:210 or .A:211 or .A:212 or .A:213 or .A:263 or .A:274 or .A:275 or .A:276 or .A:277 or .A:278; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU139
3.849
GLY140
3.564
LYS141
3.946
GLY142
3.098
LYS143
2.991
PHE144
2.990
GLY145
2.840
VAL147
3.745
ALA160
3.882
LYS162
2.791
LEU164
4.140
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| PDB ID: 6VPG TPX2 residues 7-20 fused to Aurora A residues 116-389 in complex with AMP-PNP | ||||||
| Method | X-ray diffraction | Resolution | 2.64 Å | Mutation | No | [1] |
| PDB Sequence |
SYSYDAPSDF
16 INFSSKKKRQ127 WALEDFEIGR137 PLGKGKFGNV147 YLAREKQSKF157 ILALKVLFKA 167 QLEKAGVEHQ177 LRREVEIQSH187 LRHPNILRLY197 GYFHDATRVY207 LILEYAPLGT 217 VYRELQKLSK227 FDEQRTATYI237 TELANALSYC247 HSKRVIHRDI257 KPENLLLGSA 267 GELKIADFGW277 SVHAPSSRRL289 CGTLDYLPPE299 MIEGRMHDEK309 VDLWSLGVLC 319 YEFLVGKPPF329 EANTYQETYK339 RISRVEFTFP349 DFVTEGARDL359 ISRLLKHNPS 369 QRPMLREVLE379 HPWITANSSK389
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ANP or .ANP2 or .ANP3 or :3ANP;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:194 or .A:210 or .A:211 or .A:212 or .A:213 or .A:217 or .A:258 or .A:260 or .A:261 or .A:263 or .A:274; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU139
3.402
GLY140
4.051
LYS141
3.940
GLY142
3.102
LYS143
2.337
PHE144
4.776
GLY145
4.214
VAL147
3.630
ALA160
3.445
LYS162
3.503
LEU194
3.768
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Redox priming promotes Aurora A activation during mitosis. Sci Signal. 2020 Jul 21;13(641):eabb6707. | ||||
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