Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T94823 | Target Info | |||
| Target Name | Xaa-Pro dipeptidase (PEPD) | ||||
| Synonyms | X-Pro dipeptidase; Proline dipeptidase; Prolidase; PEPD; Imidodipeptidase | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | PEPD | ||||
| Biochemical Class | Peptidase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | L-leucine | Ligand Info | |||
| Canonical SMILES | CC(C)CC(C(=O)O)N | ||||
| InChI | 1S/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1 | ||||
| InChIKey | ROHFNLRQFUQHCH-YFKPBYRVSA-N | ||||
| PubChem Compound ID | 6106 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6H2Q Crystal Structure of Arg184Gln mutant of Human Prolidase with Mn ions and LeuPro ligand | ||||||
| Method | X-ray diffraction | Resolution | 1.78 Å | Mutation | Yes | [1] |
| PDB Sequence |
GPSFWLGNET
15 LKVPLALFAL25 NRQRLCERLR35 KNPAVQAGSI45 VVLQGGEETQ55 RYCTDTGVLF 65 RQESFFHWAF75 GVTEPGCYGV85 IDVDTGKSTL95 FVPRLPASHA105 TWMGKIHSKE 115 HFKEKYAVDD125 VQYVDEIASV135 LTSQKPSVLL145 TLRGVNTDSG155 SVCREASFDG 165 ISKFEVNNTI175 LHPEIVECQV185 FKTDMELEVL195 RYTNKISSEA205 HREVMKAVKV 215 GMKEYELESL225 FEHYCYSRGG235 MRHSSYTCIC245 GSGENSAVLH255 YGHAGAPNDR 265 TIQNGDMCLF275 DMGGEYYCFA285 SDITCSFPAN295 GKFTADQKAV305 YEAVLRSSRA 315 VMGAMKPGVW325 WPDMHRLADR335 IHLEELAHMG345 ILSGSVDAMV355 QAHLGAVFMP 365 HGLGHFLGID375 VHDVGGYPEG385 VERIDEPGLR395 SLRTARHLQP405 GMVLTVEPGI 415 YFIDHLLDEA425 LADPARASFL435 NREVLQRFRG445 FGGVRIEEDV455 VVTDSGIELL 465 TCVPRTVEEI475 EACMAGCFTP487
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| PDB ID: 5M4L Crystal Structure of Wild-Type Human Prolidase with Mg ions and LeuPro ligand | ||||||
| Method | X-ray diffraction | Resolution | 1.49 Å | Mutation | No | [2] |
| PDB Sequence |
GPSFWLGNET
15 LKVPLALFAL25 NRQRLCERLR35 KNPAVQAGSI45 VVLQGGEETQ55 RYCTDTGVLF 65 RQESFFHWAF75 GVTEPGCYGV85 IDVDTGKSTL95 FVPRLPASHA105 TWMGKIHSKE 115 HFKEKYAVDD125 VQYVDEIASV135 LTSQKPSVLL145 TLRGVNTDSG155 SVCREASFDG 165 ISKFEVNNTI175 LHPEIVECRV185 FKTDMELEVL195 RYTNKISSEA205 HREVMKAVKV 215 GMKEYELESL225 FEHYCYSRGG235 MRHSSYTCIC245 GSGENSAVLH255 YGHAGAPNDR 265 TIQNGDMCLF275 DMGGEYYCFA285 SDITCSFPAN295 GKFTADQKAV305 YEAVLRSSRA 315 VMGAMKPGVW325 WPDMHRLADR335 IHLEELAHMG345 ILSGSVDAMV355 QAHLGAVFMP 365 HGLGHFLGID375 VHDVGGYPEG385 VERIDEPGLR395 SLRTARHLQP405 GMVLTVEPGI 415 YFIDHLLDEA425 LADPARASFL435 NREVLQRFRG445 FGGVRIEEDV455 VVTDSGIELL 465 TCVPRTVEEI475 EACMAGCDKA485 FTPF
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structural basis for prolidase deficiency disease mechanisms. FEBS J. 2018 Sep;285(18):3422-3441. | ||||
| REF 2 | Substrate specificity and reaction mechanism of human prolidase. FEBS J. 2017 Sep;284(17):2870-2885. | ||||
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