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 | 2-(carboxymethylamino)-2-oxoacetic acid | Ligand Info | |||
| Canonical SMILES | C(C(=O)O)NC(=O)C(=O)O | ||||
| InChI | 1S/C4H5NO5/c6-2(7)1-5-3(8)4(9)10/h1H2,(H,5,8)(H,6,7)(H,9,10) | ||||
| InChIKey | BIMZLRFONYSTPT-UHFFFAOYSA-N | ||||
| PubChem Compound ID | 3080614 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6Q9F Aspartyl/Asparaginyl beta-hydroxylase (AspH) H679A in complex with Mn, NOG and Factor X peptide fragment (39mer-4Ser) | ||||||
| Method | X-ray diffraction | Resolution | 1.63 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 MHPGTHVWPA679 TGPTNCRLRM 689 HLGLVIPKEG699 CKIRCANETK709 TWEEGKVLIF719 DDSFEHEVWQ729 DASSFRLIFI 739 VDVWHPELTP749 QQRRSLPAI
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| PDB ID: 5JQY Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine and factor X substrate peptide fragment(39mer-4Ser) | ||||||
| Method | X-ray diffraction | Resolution | 1.99 Å | Mutation | Yes | [2] |
| 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: 5JZ8 Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine, and factor X substrate peptide fragment (39mer) | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [2] |
| 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: 5JZA Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese and N-oxalylglycine | ||||||
| Method | X-ray diffraction | Resolution | 2.14 Å | Mutation | No | [2] |
| 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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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OGA or .OGA2 or .OGA3 or :3OGA;style chemicals stick;color identity;select .A:625 or .A:668 or .A:670 or .A:679 or .A:688 or .A:690 or .A:711 or .A:719 or .A:721 or .A:725 or .A:727 or .A:735 or .A:737 or .A:739; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 6RK9 Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine and cyclic peptide substrate mimic of factor X | ||||||
| Method | X-ray diffraction | Resolution | 2.29 Å | Mutation | No | [2] |
| 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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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OGA or .OGA2 or .OGA3 or :3OGA;style chemicals stick;color identity;select .A:625 or .A:627 or .A:668 or .A:670 or .A:679 or .A:688 or .A:690 or .A:711 or .A:719 or .A:721 or .A:725 or .A:727 or .A:735 or .A:737 or .A:739; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 5JZU Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine and factor X substrate peptide fragment (26mer) | ||||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | No | [2] |
| 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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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OGA or .OGA2 or .OGA3 or :3OGA;style chemicals stick;color identity;select .A:625 or .A:627 or .A:668 or .A:670 or .A:679 or .A:688 or .A:690 or .A:702 or .A:711 or .A:719 or .A:721 or .A:725 or .A:727 or .A:735 or .A:737 or .A:739; 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 | Aspartyl/Asparaginyl beta-hydroxylase (AspH) H679A in complex with Mn, NOG and Factor X peptide fragment (39mer-4Ser) | ||||
| REF 2 | Aspartate/asparagine-beta-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern. Nat Commun. 2019 Oct 28;10(1):4910. | ||||
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