Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T28265 | Target Info | |||
| Target Name | Alpha-1-antitrypsin (SERPINA1) | ||||
| Synonyms | SERPINA1; PRO0684/PRO2209; Alpha1-proteinase; Alpha-1-antiproteinase; Alpha-1 protease inhibitor | ||||
| Target Type | Successful Target | ||||
| Gene Name | SERPINA1 | ||||
| Biochemical Class | Serpin protein | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Oxamic acid | Ligand Info | |||||
| Structure Description | Crystal structure of native alpha-1-antitrypsin with seven stabilising mutations | PDB:5NBU | ||||
| Method | X-ray diffraction | Resolution | 1.67 Å | Mutation | Yes | [1] |
| PDB Sequence |
TFNKITPNLA
31 EFAFSLYRQL41 AHQSNSTNIL51 FSPVSIAAAF61 AMLSLGAKGD71 THDEILEGLN 81 FNLTEIPEAQ91 IHEGFQELLR101 TLNQSQLQLT113 TGNGLFLSEG123 LKLVDKFLED 133 VKKLYHSEAF143 TVNFGDTEEA153 KKQINDYVEK163 GTQGKIVDLV173 KELDRDTVFA 183 LVNYIFFKGK193 WERPFEVKDT203 EEEDFHVDQV213 TTVKVPMMKR223 LGMFNIQHSK 233 KLSSWVLLMK243 YLGNATAIFF253 LPDEGKLQHL263 ENELTHDIIT273 KFLENEDRRS 283 ASLHLPKLSI293 TGTYDLKSVL303 GQLGITKVFS313 NGADLSGVTE323 EAPLKLSKAV 333 HKAVLTIDEK343 GTEAAGAMFL353 EAIPMSIPPE363 VKFNKPFVFL373 IIEQNTKAPL 383 FMGRVVNPTQ393
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| Ligand Name: 3-(Trimethylsilyl)propane-1-sulfonic acid | Ligand Info | |||||
| Structure Description | Alpha-1-antitrypsin Queen's (K154N) variant | PDB:6I4V | ||||
| Method | X-ray diffraction | Resolution | 1.78 Å | Mutation | Yes | [2] |
| PDB Sequence |
NKITPNLAEF
33 AFSLYRQLAH43 QSNSTNIFFS53 PVSIATAFAM63 LSLGTKADTH73 DEILEGLNFN 83 LTEIPEAQIH93 EGFQELLRTL103 NQPDSQLQLT113 TGNGLFLSEG123 LKLVDKFLED 133 VKKLYHSEAF143 TVNFGDTEEA153 NKQINDYVEK163 GTQGKIVDLV173 KELDRDTVFA 183 LVNYIFFKGK193 WERPFEVKDT203 EEEDFHVDQV213 TTVKVPMMKR223 LGMFNIQHSK 233 KLSSWVLLMK243 YLGNATAIFF253 LPDEGKLQHL263 ENELTHDIIT273 KFLENEDRRS 283 ASLHLPKLSI293 TGTYDLKSVL303 GQLGITKVFS313 NGADLSGVTE323 EAPLKLSKAV 333 HKAVLTIDEK343 GTEAAGAMFL353 EAIPMSIPPE363 VKFNKPFVFL373 MIEQNTKSPL 383 FMGKVVNPTQ393 K
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| Ligand Name: N-[(1S,2R)-1-(3-chloro-2-methylphenyl)-1-hydroxypentan-2-yl]-2-oxo-1,3-dihydroindole-4-carboxamide | Ligand Info | |||||
| Structure Description | ALPHA-1 ANTITRYPSIN (C232S) COMPLEXED WITH cmpd 11 | PDB:7NPL | ||||
| Method | X-ray diffraction | Resolution | 1.82 Å | Mutation | No | [3] |
| PDB Sequence |
NKITPNLAEF
33 AFSLYRQLAH43 QSNSTNIFFS53 PVSIATAFAM63 LSLGTKADTH73 DEILEGLNFN 83 LTEIPEAQIH93 EGFQELLRTL103 NQPDSQLQLT113 TGNGLFLSEG123 LKLVDKFLED 133 VKKLYHSEAF143 TVNFGDTEEA153 KKQINDYVEK163 GTQGKIVDLV173 KELDRDTVFA 183 LVNYIFFKGK193 WERPFEVKDT203 EEEDFHVDQV213 TTVKVPMMKR223 LGMFNIQHSK 233 KLSSWVLLMK243 YLGNATAIFF253 LPDEGKLQHL263 ENELTHDIIT273 KFLENEDRRS 283 ASLHLPKLSI293 TGTYDLKSVL303 GQLGITKVFS313 NGADLSGVTE323 EAPLKLSKAV 333 HKAVLTIDEP357 MSIPPEVKFN367 KPFVFLMIEQ377 NTKSPLFMGK387 VVNPTQK |
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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 .UKZ or .UKZ2 or .UKZ3 or :3UKZ;style chemicals stick;color identity;select .A:192 or .A:193 or .A:194 or .A:198 or .A:221 or .A:244 or .A:250 or .A:252 or .A:288 or .A:289 or .A:290 or .A:291 or .A:292 or .A:293 or .A:338 or .A:340 or .A:342 or .A:366 or .A:370 or .A:372 or .A:374 or .A:388; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
GLY192
4.338
LYS193
3.402
TRP194
2.874
PHE198
3.947
MET221
3.626
TYR244
2.595
ALA250
4.260
PHE252
3.703
LEU288
3.684
PRO289
2.954
LYS290
3.544
|
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| Ligand Name: N-((1S,2R)-1-hydroxy-1-(o-tolyl)pentan-2-yl)-2-oxo-2,3-dihydrobenzo[d]oxazole-5-carboxamide | Ligand Info | |||||
| Structure Description | ALPHA-1 ANTITRYPSIN C232S COMPLEXED WITH CMPD3 | PDB:7NPK | ||||
| Method | X-ray diffraction | Resolution | 1.83 Å | Mutation | Yes | [3] |
| PDB Sequence |
TFNKITPNLA
31 EFAFSLYRQL41 AHQSNSTNIF51 FSPVSIATAF61 AMLSLGTKAD71 THDEILEGLN 81 FNLTEIPEAQ91 IHEGFQELLR101 TLNQPDSQLQ111 LTTGNGLFLS121 EGLKLVDKFL 131 EDVKKLYHSE141 AFTVNFGDTE151 EAKKQINDYV161 EKGTQGKIVD171 LVKELDRDTV 181 FALVNYIFFK191 GKWERDTEEE206 DFHVDQVTTV216 KVPMMKRLGM226 FNIQHSKKLS 236 SWVLLMKYLG246 NATAIFFLPD256 EGKLQHLENE266 LTHDIITKFL276 ENEDRRSASL 286 HLPKLSITGT296 YDLKSVLGQL306 GITKVFSNGA316 DLSGVTEEAP326 LKLSKAVHKA 336 VLTIDPMSIP361 PEVKFNKPFV371 FLMIEQNTKS381 PLFMGKVVNP391 TQ |
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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 .UL2 or .UL22 or .UL23 or :3UL2;style chemicals stick;color identity;select .A:51 or .A:194 or .A:203 or .A:221 or .A:242 or .A:244 or .A:250 or .A:252 or .A:288 or .A:289 or .A:290 or .A:291 or .A:292 or .A:293 or .A:338 or .A:340 or .A:366 or .A:370 or .A:372 or .A:374 or .A:388; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
PHE51
4.996
TRP194
3.416
THR203
4.019
MET221
3.562
MET242
4.252
TYR244
2.720
ALA250
4.948
PHE252
3.720
LEU288
3.533
PRO289
3.018
LYS290
3.601
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | CRYSTAL STRUCTURE OF THE Z VARIANT OF ALPHA-1-ANTITRYPSIN REVEALS STRUCTURAL AND DYNAMICAL CHANGES AND SUPPORTS A C-TERMINAL DOMAIN SWAP MECHANISM OF POLYMERIZATION | ||||
| REF 2 | Structural determinants of instability in alpha-1-antitrypsin | ||||
| REF 3 | The development of highly potent and selective small molecule correctors of Z Alpha(1)-antitrypsin misfolding. Bioorg Med Chem Lett. 2021 Jun 1;41:127973. | ||||
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