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 | (2R,3S,4R,5R,6R)-2,6-difluoro-2-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol | Ligand Info | |||
| Canonical SMILES | C(C1(C(C(C(C(O1)F)O)O)O)F)O | ||||
| InChI | 1S/C6H10F2O5/c7-5-3(11)2(10)4(12)6(8,1-9)13-5/h2-5,9-12H,1H2/t2-,3-,4+,5+,6+/m1/s1 | ||||
| InChIKey | MGHYRMVVRYCAON-PQMKYFCFSA-N | ||||
| PubChem Compound ID | 44241503 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 3IJ8 Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase | ||||||
| Method | X-ray diffraction | Resolution | 1.43 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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LYS140
2.830
TYR151
4.186
LEU162
4.105
GLU171
3.849
ARG176
3.870
ARG195
4.840
ASP197
4.657
ALA198
3.475
LYS200
4.582
HIS201
2.519
TRP203
3.257
PRO204
3.598
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| PDB ID: 3IJ9 Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase | ||||||
| Method | X-ray diffraction | Resolution | 1.85 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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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Directed "in situ" inhibitor elongation as a strategy to structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic alpha-amylase. Biochemistry. 2009 Nov 17;48(45):10752-64. | ||||
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