Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T21678 | Target Info | |||
| Target Name | Alpha-galactosidase A (GLA) | ||||
| Synonyms | Melibiase; INN=Agalsidase; Alpha-D-galactoside galactohydrolase; Alpha-D-galactosidase A | ||||
| Target Type | Successful Target | ||||
| Gene Name | GLA | ||||
| Biochemical Class | Glycosylase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Levovist | Ligand Info | |||
| Canonical SMILES | C(C1C(C(C(C(O1)O)O)O)O)O | ||||
| InChI | 1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3+,4+,5-,6+/m1/s1 | ||||
| InChIKey | WQZGKKKJIJFFOK-PHYPRBDBSA-N | ||||
| PubChem Compound ID | 439357 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 3LXA Interconversion of Human Lysosomal Enzyme Specificities | ||||||
| Method | X-ray diffraction | Resolution | 3.04 Å | Mutation | Yes | [1] |
| PDB Sequence |
LDNGLARTPT
41 MGWLHWERFM51 CNLDCQEEPD61 SCISEKLFME71 MAELMVSEGW81 KDAGYEYLCI 91 DDCWMAPQRD101 SEGRLQADPQ111 RFPHGIRQLA121 NYVHSKGLKL131 GIYADVGNKT 141 CAGFPGSFGY151 YDIDAQTFAD161 WGVDLLKFDG171 CYCDSLENLA181 DGYKHMSLAL 191 NRTGRSIVYS201 CSWPAYMWPF211 QKPNYTEIRQ221 YCNHWRNFAD231 IDDSWKSIKS 241 ILDWTSFNQE251 RIVDVAGPGG261 WNDPDMLVIG271 NFGLSWNQQV281 TQMALWAIMA 291 APLFMSNDLR301 HISPQAKALL311 QDKDVIAINQ321 DPLGKQGYQL331 RQGDNFEVWE 341 RPLSGLAWAV351 AMINRQEIGG361 PRSYTIAVAS371 LGKGVACNPA381 CFITQLLPVK 391 RKLGFYEWTS401 RLRSHINPTG411 TVLLQLENTM421 QMSLK
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TRP47
3.491
ASP92
2.841
ASP93
2.883
TYR134
3.159
CYS142
2.984
ALA143
3.609
LYS168
2.856
ASP170
2.921
TYR207
3.983
ARG227
3.036
ASP231
2.401
|
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| PDB ID: 3S5Z Pharmacological Chaperoning in Human alpha-Galactosidase | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [2] |
| PDB Sequence |
LDNGLARTPT
41 MGWLHWERFM51 CNLDCQEEPD61 SCISEKLFME71 MAELMVSEGW81 KDAGYEYLCI 91 DDCWMAPQRD101 SEGRLQADPQ111 RFPHGIRQLA121 NYVHSKGLKL131 GIYADVGNKT 141 CAGFPGSFGY151 YDIDAQTFAD161 WGVDLLKFDG171 CYCDSLENLA181 DGYKHMSLAL 191 NRTGRSIVYS201 CEWPLYMWPF211 QKPNYTEIRQ221 YCNHWRNFAD231 IDDSWKSIKS 241 ILDWTSFNQE251 RIVDVAGPGG261 WNDPDMLVIG271 NFGLSWNQQV281 TQMALWAIMA 291 APLFMSNDLR301 HISPQAKALL311 QDKDVIAINQ321 DPLGKQGYQL331 RQGDNFEVWE 341 RPLSGLAWAV351 AMINRQEIGG361 PRSYTIAVAS371 LGKGVACNPA381 CFITQLLPVK 391 RKLGFYEWTS401 RLRSHINPTG411 TVLLQLENTM421
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| PDB ID: 3GXP Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 | ||||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | No | [3] |
| PDB Sequence |
LDNGLARTPT
41 MGWLHWERFM51 CNLDCQEEPD61 SCISEKLFME71 MAELMVSEGW81 KDAGYEYLCI 91 DDCWMAPQRD101 SEGRLQADPQ111 RFPHGIRQLA121 NYVHSKGLKL131 GIYADVGNKT 141 CAGFPGSFGY151 YDIDAQTFAD161 WGVDLLKFDG171 CYCDSLENLA181 DGYKHMSLAL 191 NRTGRSIVYS201 CEWPLYMWPF211 QKPNYTEIRQ221 YCNHWRNFAD231 IDDSWKSIKS 241 ILDWTSFNQE251 RIVDVAGPGG261 WNDPDMLVIG271 NFGLSWNQQV281 TQMALWAIMA 291 APLFMSNDLR301 HISPQAKALL311 QDKDVIAINQ321 DPLGKQGYQL331 RQGDNFEVWE 341 RPLSGLAWAV351 AMINRQEIGG361 PRSYTIAVAS371 LGKGVACNPA381 CFITQLLPVK 391 RKLGFYEWTS401 RLRSHINPTG411 TVLLQLENTM421
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| PDB ID: 3HG5 Human alpha-galactosidase catalytic mechanism 4. Product bound | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [4] |
| PDB Sequence |
LDNGLARTPT
41 MGWLHWERFM51 CNLDCQEEPD61 SCISEKLFME71 MAELMVSEGW81 KDAGYEYLCI 91 DDCWMAPQRD101 SEGRLQADPQ111 RFPHGIRQLA121 NYVHSKGLKL131 GIYADVGNKT 141 CAGFPGSFGY151 YDIDAQTFAD161 WGVDLLKFDG171 CYCDSLENLA181 DGYKHMSLAL 191 NRTGRSIVYS201 CEWPLYMWPF211 QKPNYTEIRQ221 YCNHWRNFAD231 IDDSWKSIKS 241 ILDWTSFNQE251 RIVDVAGPGG261 WNDPDMLVIG271 NFGLSWNQQV281 TQMALWAIMA 291 APLFMSNDLR301 HISPQAKALL311 QDKDVIAINQ321 DPLGKQGYQL331 RQGDNFEVWE 341 RPLSGLAWAV351 AMINRQEIGG361 PRSYTIAVAS371 LGKGVACNPA381 CFITQLLPVK 391 RKLGFYEWTS401 RLRSHINPTG411 TVLLQLENTM421
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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 .GLA or .GLA2 or .GLA3 or :3GLA;style chemicals stick;color identity;select .A:47 or .A:92 or .A:93 or .A:134 or .A:142 or .A:143 or .A:168 or .A:170 or .A:203 or .A:206 or .A:207 or .A:227 or .A:231 or .A:266 or .A:267; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases. J Biol Chem. 2010 Jul 9;285(28):21560-6. | ||||
| REF 2 | The molecular basis of pharmacological chaperoning in human Alpha-galactosidase. Chem Biol. 2011 Dec 23;18(12):1521-6. | ||||
| REF 3 | Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability. Biochemistry. 2009 Jun 9;48(22):4816-27. | ||||
| REF 4 | Catalytic mechanism of human alpha-galactosidase. J Biol Chem. 2010 Feb 5;285(6):3625-3632. | ||||
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