Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T52133 | Target Info | |||
| Target Name | Aspartate beta-hydroxylase (ASPH) | ||||
| Synonyms | Peptideaspartate betadioxygenase; Aspartyl/asparaginyl betahydroxylase; ASPH; ASP betahydroxylase | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | ASPH | ||||
| Biochemical Class | Paired donor oxygen oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | (3~{R})-3-methyl-2-oxidanylidene-pentanedioic acid | Ligand Info | |||
| Canonical SMILES | CC(CC(=O)O)C(=O)C(=O)O | ||||
| InChI | 1S/C6H8O5/c1-3(2-4(7)8)5(9)6(10)11/h3H,2H2,1H3,(H,7,8)(H,10,11)/t3-/m1/s1 | ||||
| InChIKey | BJQIUPTURRAODO-GSVOUGTGSA-N | ||||
| PubChem Compound ID | 23642650 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6YYX Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with manganese, 3-methyl-2-oxoglutarate, and factor X substrate peptide fragment(39mer-4Ser) | ||||||
| Method | X-ray diffraction | Resolution | 1.53 Å | Mutation | Yes | [1] |
| PDB Sequence |
KPKLLNKFDK
339 TIKAELDAAE349 KLRKRGKIEE359 AVNAFKELVR369 KYPQSPRARY379 GKAQCEDDLA 389 EKRRSNEVLR399 GAIETYQEVA409 SLPDVPADLL419 KLSLKRRSDR429 QQFLGHMRGS 439 LLTLQRLVQL449 FPNDTSLKND459 LGVGYLLIGD469 NDNAKKVYEE479 VLSVTPNDGF 489 AKVHYGFILK499 AQNKIAESIP509 YLKEGIESGD519 PGTDDGRFYF529 HLGDAMQRVG 539 NKEAYKWYEL549 GHKRGHFASV559 WQRSLYNVNG569 LKAQPWWTPK579 ETGYTELVKS 589 LERNWKLIRD599 EGLAVMDKAK609 GLFLPEDENL619 REKGDWSQFT629 LWQQGRRNEN 639 ACKGAPKTCT649 LLEKFPETTG659 CRRGQIKYSI669 MHPGTHVWPH679 TGPTNCRLRM 689 HLGLVIPKEG699 CKIRCANETK709 TWEEGKVLIF719 DDSFEHEVWQ729 DASSFRLIFI 739 VDVWHPELTP749 QQRRSLPAI
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| PDB ID: 6YYV Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with manganese and 3-methyl-2-oxoglutarate | ||||||
| Method | X-ray diffraction | Resolution | 1.77 Å | Mutation | No | [1] |
| PDB Sequence |
KPKLLNKFDK
339 TIKAELDAAE349 KLRKRGKIEE359 AVNAFKELVR369 KYPQSPRARY379 GKAQCEDDLA 389 EKRRSNEVLR399 GAIETYQEVA409 SLPDVPADLL419 KLSLKRRSDR429 QQFLGHMRGS 439 LLTLQRLVQL449 FPNDTSLKND459 LGVGYLLIGD469 NDNAKKVYEE479 VLSVTPNDGF 489 AKVHYGFILK499 AQNKIAESIP509 YLKEGIESGD519 PGTDDGRFYF529 HLGDAMQRVG 539 NKEAYKWYEL549 GHKRGHFASV559 WQRSLYNVNG569 LKAQPWWTPK579 ETGYTELVKS 589 LERNWKLIRD599 EGLAVMDKAK609 GLFLPEDENL619 REKGDWSQFT629 LWQQGRRNEN 639 ACKGAPKTCT649 LLEKFPETTG659 CRRGQIKYSI669 MHPGTHVWPH679 TGPTNCRLRM 689 HLGLVIPKEG699 CKIRCANETK709 TWEEGKVLIF719 DDSFEHEVWQ729 DASSFRLIFI 739 VDVWHPELTP749 QQRRSLPAI
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Synthesis of 2-oxoglutarate derivatives and their evaluation as cosubstrates and inhibitors of human aspartate/asparagine-beta-hydroxylase. doi:10.1039/D0SC04301J. | ||||
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