7FW5
Crystal Structure of human FABP4 with active site mutated to that of FABP3 in complex with palmitate
Summary for 7FW5
| Entry DOI | 10.2210/pdb7fw5/pdb |
| Group deposition | To be published (G_1002264) |
| Descriptor | Fatty acid-binding protein, adipocyte, PALMITIC ACID (3 entities in total) |
| Functional Keywords | lipid binding protein, fatty acid binding protein, cytoplasm, lipid-binding, transport, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15316.67 |
| Authors | Ehler, A.,Benz, J.,Obst, U.,Rudolph, M.G. (deposition date: 2023-04-27, release date: 2023-06-14, Last modification date: 2025-08-13) |
| Primary citation | Ehler, A.,Bartelmus, C.,Benz, J.,Plitzko, I.,Rudolph, M.G. A high-resolution data set of fatty acid-binding protein structures. III. Unexpectedly high occurrence of wrong ligands. Acta Crystallogr D Struct Biol, 81:451-464, 2025 Cited by PubMed Abstract: FABP4 has been implicated as a therapeutic target for treating diabetes and atherosclerosis. Structure-based drug design (SBDD) based on initial hits from high-throughput and fragment screens yielded 216 ligand-bound structures of human FABP3, FABP4 and FABP5 isoforms, many of which were at resolutions of better than 1.2 Å. An estimated 15% of the ligands had a different chemical composition to that expected from the starting materials or the final synthesis product, highlighting a potential problem inherent to all SBDD campaigns conducted at lower resolution. Apart from possible human error during compound registration, side reactions such as additions, eliminations, isomerizations, cyclizations and dimerizations were found that led to compounds capable of binding to FABP. PubMed: 40748031DOI: 10.1107/S2059798325006096 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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