Entry | Database: PDB / ID: 4z50 |
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Title | Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20D25N with Tucked Flap |
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Components | Protease |
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Keywords | HYDROLASE / HIV-1 Protease |
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Function / homology | Function and homology information
Retropepsin-like catalytic domain / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Cathepsin D, subunit A; domain 1 / Acid Proteases / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily ...Retropepsin-like catalytic domain / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Cathepsin D, subunit A; domain 1 / Acid Proteases / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Beta Barrel / Mainly BetaSimilarity search - Domain/homology |
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Biological species | ![](img/tx_virus.gif) ![](data/emdb/media/1155/snaps2.jpg) Human immunodeficiency virus 1 |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å |
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Authors | Agniswamy, J. / Shen, C.-H. / Weber, I.T. |
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Funding support | United States, 1items Organization | Grant number | Country |
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National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | U01GM062920 | United States |
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Citation | Journal: J.Mol.Graph.Model. / Year: 2015 Title: Conformational variation of an extreme drug resistant mutant of HIV protease. Authors: Shen, C.H. / Chang, Y.C. / Agniswamy, J. / Harrison, R.W. / Weber, I.T. |
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History | Deposition | Apr 2, 2015 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Oct 14, 2015 | Provider: repository / Type: Initial release |
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Revision 1.1 | Sep 27, 2017 | Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation |
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Revision 1.2 | Dec 25, 2019 | Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization |
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Revision 1.3 | Sep 27, 2023 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_symmetry |
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