Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T86918 | Target Info | |||
| Target Name | Pancreatic alpha-amylase (AMY2A) | ||||
| Synonyms | PA; 1,4-alpha-D-glucan glucanohydrolase | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | AMY2A | ||||
| Biochemical Class | Glycosylase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Acarbose derived pentasaccharide | Ligand Info | |||
| Canonical SMILES | CC1C(C(C(C(O1)OC2C(OC(C(C2O)O)O)CO)O)O)NC3C=C(C(C(C3O)O)OC4C(C(C(C(O4)CO)OC5C(C(C(C(O5)CO)O)O)O)O)O)CO | ||||
| InChI | 1S/C31H53NO23/c1-7-13(16(39)22(45)29(49-7)54-26-11(5-35)50-28(48)21(44)19(26)42)32-9-2-8(3-33)25(18(41)14(9)37)53-31-24(47)20(43)27(12(6-36)52-31)55-30-23(46)17(40)15(38)10(4-34)51-30/h2,7,9-48H,3-6H2,1H3/t7-,9+,10-,11-,12-,13-,14+,15-,16+,17+,18-,19-,20-,21-,22-,23-,24-,25-,26-,27-,28+,29-,30-,31-/m1/s1 | ||||
| InChIKey | JUCZMZWYUIRMPL-NPPSNIQKSA-N | ||||
| PubChem Compound ID | 4369394 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 3BAY N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose | ||||||
| Method | X-ray diffraction | Resolution | 1.99 Å | Mutation | Yes | [1] |
| PDB Sequence |
YSPNTQQGRT
11 SIVHLFEWRW21 VDIALECERY31 LAPKGFGGVQ41 VSPPNENVAI51 YNPFRPWWER 61 YQPVSYKLCT71 RSGNEDEFRN81 MVTRCNNVGV91 RIYVDAVINH101 MCGNAVSAGT 111 SSTCGSYFNP121 GSRDFPAVPY131 SGWDFNDGKC141 KTGSGDIENY151 NDATQVRDCR 161 LTGLLDLALE171 KDYVRSKIAE181 YMNHLIDIGV191 AGFRLDASKH201 MWPGDIKAIL 211 DKLHNLNSNW221 FPAGSKPFIY231 QEVIDLGGEP241 IKSSDYFGNG251 RVTEFKYGAK 261 LGTVIRKWNG271 EKMSYLKNWG281 EGWGFVPSDR291 ALVFVDSHDN301 QRGHGAGGAS 311 ILTFWDARLY321 KMAVGFMLAH331 PYGFTRVMSS341 YRWPRQFQNG351 NDVNDWVGPP 361 NNNGVIKEVT371 INPDTTCGND381 WVCEHRWRQI391 RNMVIFRNVV401 DGQPFTNWYD 411 NGSNQVAFGR421 GNRGFIVFNN431 DDWSFSLTLQ441 TGLPAGTYCD451 VISGDKINGN 461 CTGIKIYVSD471 DGKAHFSISN481 SAEDPFIAIH491 AESKL
|
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|
|
TRP58
3.258
TRP59
2.805
GLU60
4.780
TYR62
3.349
GLN63
3.060
HIS101
2.904
GLY104
3.816
TYR151
3.349
LEU162
3.538
THR163
2.661
GLY164
3.783
LEU165
3.100
ARG195
2.798
|
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| PDB ID: 1XD0 Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [2] |
| PDB Sequence |
YSPNTQQGRT
11 SIVHLFEWRW21 VDIALECERY31 LAPKGFGGVQ41 VSPPNENVAI51 YNPFRPWWER 61 YQPVSYKLCT71 RSGNEDEFRN81 MVTRCNNVGV91 RIYVDAVINH101 MCGNAVSAGT 111 SSTCGSYFNP121 GSRDFPAVPY131 SGWDFNDGKC141 KTGSGDIENY151 NDATQVRDCR 161 LTGLLDLALE171 KDYVRSKIAE181 YMNHLIDIGV191 AGFRLDASKH201 MWPGDIKAIL 211 DKLHNLNSNW221 FPAGSKPFIY231 QEVIDLGGEP241 IKSSDYFGNG251 RVTEFKYGAK 261 LGTVIRKWNG271 EKMSYLKNWG281 EGWGFVPSDR291 ALVFVDNHDN301 QRGHGAGGAS 311 ILTFWDARLY321 KMAVGFMLAH331 PYGFTRVMSS341 YRWPRQFQNG351 NDVNDWVGPP 361 NNNGVIKEVT371 INPDTTCGND381 WVCEHRWRQI391 RNMVIFRNVV401 DGQPFTNWYD 411 NGSNQVAFGR421 GNRGFIVFNN431 DDWSFSLTLQ441 TGLPAGTYCD451 VISGDKINGN 461 CTGIKIYVSD471 DGKAHFSISN481 SAEDPFIAIH491 AESKL
|
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|
|
TRP58
3.309
TRP59
2.621
GLU60
4.420
TYR62
3.464
GLN63
2.935
VAL98
4.453
HIS101
3.045
GLY104
3.871
ASN105
4.979
TYR151
3.503
LEU162
3.765
THR163
2.768
GLY164
4.086
LEU165
3.872
|
|||||
| PDB ID: 3BAJ Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [1] |
| PDB Sequence |
YSPNTQQGRT
11 SIVHLFEWRW21 VDIALECERY31 LAPKGFGGVQ41 VSPPNENVAI51 YNPFRPWWER 61 YQPVSYKLCT71 RSGNEDEFRN81 MVTRCNNVGV91 RIYVDAVINH101 MCGNAVSAGT 111 SSTCGSYFNP121 GSRDFPAVPY131 SGWDFNDGKC141 KTGSGDIENY151 NDATQVRDCR 161 LTGLLDLALE171 KDYVRSKIAE181 YMNHLIDIGV191 AGFRLDASKH201 MWPGDIKAIL 211 DKLHNLNSNW221 FPAGSKPFIY231 QEVIDLGGEP241 IKSSDYFGNG251 RVTEFKYGAK 261 LGTVIRKWNG271 EKMSYLKNWG281 EGWGFVPSDR291 ALVFVDNHDN301 QRGHGAGGAS 311 ILTFWDARLY321 KMAVGFMLAH331 PYGFTRVMSS341 YRWPRQFQNG351 NDVNDWVGPP 361 NNNGVIKEVT371 INPDTTCGND381 WVCEHRWRQI391 RNMVIFRNVV401 DGQPFTNWYD 411 NGSNQVAFGR421 GNRGFIVFNN431 DDWSFSLTLQ441 TGLPAGTYCD451 VISGDKINGN 461 CTGIKIYVSD471 DGKAHFSISN481 SAEDPFIAIH491 AESKL
|
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|
|
TRP58
3.365
TRP59
2.978
GLU60
4.879
TYR62
3.513
GLN63
2.874
HIS101
2.868
GLY104
3.944
TYR151
3.693
LEU162
3.564
THR163
2.718
GLY164
4.091
LEU165
3.412
ARG195
2.824
|
|||||
| PDB ID: 1XH2 Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose | ||||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [3] |
| PDB Sequence |
YSPNTQQGRT
11 SIVHLFEWRW21 VDIALECERY31 LAPKGFGGVQ41 VSPPNENVAI51 YNPFRPWWER 61 YQPVSYKLCT71 RSGNEDEFRN81 MVTRCNNVGV91 RIYVDAVINH101 MCGNAVSAGT 111 SSTCGSYFNP121 GSRDFPAVPY131 SGWDFNDGKC141 KTGSGDIENY151 NDATQVRDCR 161 LTGLLDLALE171 KDYVRSKIAE181 YMNHLIDIGV191 AGFRLDASKH201 MWPGDIKAIL 211 DKLHNLNSNW221 FPAGSKPFIY231 QEVIDLGGEP241 IKSSDYFGNG251 RVTEFKYGAK 261 LGTVIRKWNG271 EKMSYLKNWG281 EGWGFVPSDR291 ALVFVDSHDN301 QRGHGAGGAS 311 ILTFWDARLY321 KMAVGFMLAH331 PYGFTRVMSS341 YRWPRQFQNG351 NDVNDWVGPP 361 NNNGVIKEVT371 INPDTTCGND381 WVCEHRWRQI391 RNMVIFRNVV401 DGQPFTNWYD 411 NGSNQVAFGR421 GNRGFIVFNN431 DDWSFSLTLQ441 TGLPAGTYCD451 VISGDKINGN 461 CTGIKIYVSD471 DGKAHFSISN481 SAEDPFIAIH491 AESKL
|
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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 .ARE or .ARE2 or .ARE3 or :3ARE;style chemicals stick;color identity;select .A:58 or .A:59 or .A:60 or .A:62 or .A:63 or .A:98 or .A:101 or .A:104 or .A:105 or .A:151 or .A:162 or .A:163 or .A:164 or .A:165 or .A:195 or .A:197 or .A:198 or .A:200 or .A:201 or .A:233 or .A:235 or .A:240 or .A:299 or .A:300 or .A:305 or .A:307; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
TRP58
3.324
TRP59
2.697
GLU60
4.567
TYR62
3.596
GLN63
2.993
VAL98
4.711
HIS101
2.743
GLY104
3.715
ASN105
4.859
TYR151
3.680
LEU162
3.700
THR163
2.913
GLY164
3.983
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity. Biochemistry. 2008 Mar 18;47(11):3332-44. | ||||
| REF 2 | Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts. Biochemistry. 2005 Mar 8;44(9):3347-57. | ||||
| REF 3 | Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase. Protein Sci. 2005 Mar;14(3):743-55. | ||||
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