Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T78277 | Target Info | |||
| Target Name | Asparaginase (ASRGL1) | ||||
| Synonyms | Lasparagine amidohydrolase; Isoaspartyl peptidase/Lasparaginase beta chain; Isoaspartyl peptidase/Lasparaginase; Isoaspartyl dipeptidase; Betaaspartylpeptidase; Asparaginaselike protein 1; ASRGL1 | ||||
| Target Type | Successful Target | ||||
| Gene Name | ASRGL1 | ||||
| Biochemical Class | Peptidase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
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| Ligand Name: L-aspartic acid | Ligand Info | |||||
| Structure Description | Crystal structure of human L-asparaginase protein with covalently linked substrate L-asparagine | PDB:4O0H | ||||
| Method | X-ray diffraction | Resolution | 1.97 Å | Mutation | No | [1] |
| PDB Sequence |
HMNPIVVVHG
9 GGAGPISKDR19 KERVHQGMVR29 AATVGYGILR39 EGGSAVDAVE49 GAVVALEDDP 59 EFNAGCGSVL69 NTNGEVEMDA79 SIMDGKDLSA89 GAVSAVQCIA99 NPIKLARLVM 109 EKTPHCFLTD119 QGAAQFAAAM129 GVPEIPGEKL139 VTERNKKRLE149 KEKHTVGAVA 173 LDCKGNVAYA183 TSTGGIVNKM193 VGRVGDSPCL203 GAGGYADNDI213 GAVSTTGHGE 223 SILKVNLARL233 TLFHIEQGKT243 VEEAADLSLG253 YMKSRVKGLG263 GLIVVSKTGD 273 WVAKWTSTSM283 PWAAAKDGKL293 HFGIDPDDTT303 ITDLP
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| Ligand Name: L-aspartic acid | Ligand Info | |||||
| Structure Description | Crystal structure of partially-cleaved human l-asparaginase protein in complex with l-aspartate | PDB:4PVR | ||||
| Method | X-ray diffraction | Resolution | 1.75 Å | Mutation | No | [2] |
| PDB Sequence |
HMNPIVVVHG
9 GGAGPISKDR19 KERVHQGMVR29 AATVGYGILR39 EGGSAVDAVE49 GAVVALEDDP 59 EFNAGCGSVL69 NTNGEVEMDA79 SIMDGKDLSA89 GAVSAVQCIA99 NPIKLARLVM 109 EKTPHCFLTD119 QGAAQFAAAM129 GVPEIPGEKL139 VTERNKKRLE149 KEKHNLGTVG 170 AVALDCKGNV180 AYATSTGGIV190 NKMVGRVGDS200 PCLGAGGYAD210 NDIGAVSTTG 220 HGESILKVNL230 ARLTLFHIEQ240 GKTVEEAADL250 SLGYMKSRVK260 GLGGLIVVSK 270 TGDWVAKWTS280 TSMPWAAAKD290 GKLHFGIDPD300 DTTITDLP
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Tris(hydroxyethyl)aminomethane | Ligand Info | |||||
| Structure Description | Crystal Structure of Human Asparaginase-like Protein 1 Thr168Ala | PDB:3TKJ | ||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | Yes | [3] |
| PDB Sequence |
GNPIVVVHGG
10 GAGPISKDRK20 ERVHQGMVRA30 ATVGYGILRE40 GGSAVDAVEG50 AVVALEDDPE 60 FNAGCGSVLN70 TNGEVEMDAS80 IMDGKDLSAG90 AVSAVQCIAN100 PIKLARLVME 110 KTPHCFLTDQ120 GAAQFAAAMG130 VPEIPGEKLV140 TERNKKRLEK150 EKHELGAVGA 171 VALDCKGNVA181 YATSTGGIVN191 KMVGRVGDSP201 CLGAGGYADN211 DIGAVSTTGH 221 GESILKVNLA231 RLTLFHIEQG241 KTVEEAADLS251 LGYMKSRVKG261 LGGLIVVSKT 271 GDWVAKWTST281 SMPWAAAKDG291 KLHFGIDPDD301 TTITDLP
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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 .TAM or .TAM2 or .TAM3 or :3TAM;style chemicals stick;color identity;select .A:1 or .A:2 or .A:3 or .A:35 or .A:38 or .A:39 or .A:176 or .A:290; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Elucidation of the specific function of the conserved threonine triad responsible for human L-asparaginase autocleavage and substrate hydrolysis. J Mol Biol. 2014 Jun 26;426(13):2471-85. | ||||
| REF 2 | Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis. Biochemistry. 2012 Aug 28;51(34):6816-26. | ||||
| REF 3 | Uncoupling intramolecular processing and substrate hydrolysis in the N-terminal nucleophile hydrolase hASRGL1 by circular permutation. ACS Chem Biol. 2012 Nov 16;7(11):1840-7. | ||||
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