Entry | Database: PDB / ID: 4r4y |
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Title | Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria |
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Components | N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase |
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Keywords | HYDROLASE / AGU structure / autoprocessing / glycosylasparaginase / lysosomal storage disease / pre-autoproteolysis trap |
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Function / homology | Function and homology information
N4-(beta-N-acetylglucosaminyl)-L-asparaginase / N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity / asparaginase activity / beta-aspartyl-peptidase activity / periplasmic space / lysosome / proteolysisSimilarity search - Function Peptidase T2, asparaginase 2 / Asparaginase / Twin-arginine translocation pathway, signal sequence, bacterial/archaeal / Nucleophile aminohydrolases, N-terminalSimilarity search - Domain/homology |
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Biological species | Elizabethkingia miricola (bacteria) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å |
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Authors | Sui, L. / Damodharan, L. / Pande, S. / Guo, H.C. |
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Citation | Journal: Structure / Year: 2014 Title: Structural Basis of a Point Mutation that Causes the Genetic Disease Aspartylglucosaminuria. Authors: Sui, L. / Lakshminarasimhan, D. / Pande, S. / Guo, H.C. |
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History | Deposition | Aug 20, 2014 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Dec 17, 2014 | Provider: repository / Type: Initial release |
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Revision 1.1 | Feb 28, 2024 | Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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