Entry | Database: PDB / ID: 3zu4 |
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Title | Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH and the 2-pyridone inhibitor PT172 |
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Components | PUTATIVE REDUCTASE YPO4104/Y4119/YP_4011 |
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Keywords | OXIDOREDUCTASE / FATTY ACID BIOSYNTHESIS II / SHORT-CHAIN DEHYDROGENASE REDUCTASE SUPERFAMILY |
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Function / homology | Function and homology information
trans-2-enoyl-CoA reductase (NADH) activity / enoyl-[acyl-carrier-protein] reductase (NADH) / enoyl-[acyl-carrier-protein] reductase (NADH) activity / fatty acid biosynthetic process / NAD bindingSimilarity search - Function Trans-2-enoyl-CoA reductase / Enoyl reductase FAD binding domain / Trans-2-enoyl-CoA reductase catalytic domain, putative / Enoyl reductase FAD binding domain / Trans-2-enoyl-CoA reductase catalytic region / NAD(P)H binding domain of trans-2-enoyl-CoA reductase / NAD(P)-binding Rossmann-like Domain / Rossmann fold / 3-Layer(aba) Sandwich / Alpha BetaSimilarity search - Domain/homology 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / 1-(2-CHLOROBENZYL)-4-HEXYLPYRIDIN-2(1H)-ONE / Enoyl-[acyl-carrier-protein] reductase [NADH]Similarity search - Component |
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Biological species | ![](img/tx_bacteria.gif) YERSINIA PESTIS (bacteria) |
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Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.01 Å |
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Authors | Hirschbeck, M.W. / Kuper, J. / Tonge, P.J. / Kisker, C. |
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Citation | Journal: Structure / Year: 2012 Title: Structure of the Yersinia Pestis Fabv Enoyl-Acp Reductase and its Interaction with Two 2-Pyridone Inhibitors Authors: Hirschbeck, M.W. / Kuper, J. / Lu, H. / Liu, N. / Neckles, C. / Shah, S. / Wagner, S. / Sotriffer, C.A. / Tonge, P.J. / Kisker, C. |
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History | Deposition | Jul 13, 2011 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Jan 18, 2012 | Provider: repository / Type: Initial release |
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Revision 1.1 | Mar 28, 2012 | Group: Other |
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Revision 1.2 | Jul 5, 2017 | Group: Data collection / Category: diffrn_source / Item: _diffrn_source.type |
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Revision 1.3 | May 8, 2024 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_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_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_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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