4RUN
Crystal structure of human odorant binding protein OBPIIa
Summary for 4RUN
| Entry DOI | 10.2210/pdb4run/pdb |
| Descriptor | Odorant-binding protein 2a, CITRATE ANION (3 entities in total) |
| Functional Keywords | human lipocalin, lipid binding protein, odorant binding protein, vanillin, lilial, fatty acids, aliphatic aldehydes, nasal mucus, transport protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted : Q9NY56 |
| Total number of polymer chains | 2 |
| Total formula weight | 37499.66 |
| Authors | Schiefner, A.,Skerra, A. (deposition date: 2014-11-21, release date: 2015-04-08, Last modification date: 2024-11-27) |
| Primary citation | Schiefner, A.,Freier, R.,Eichinger, A.,Skerra, A. Crystal structure of the human odorant binding protein, OBPIIa. Proteins, 83:1180-1184, 2015 Cited by PubMed Abstract: Human odorant-binding protein, OBPIIa , is expressed by nasal epithelia to facilitate transport of hydrophobic odorant molecules across the aqueous mucus. Here, we report its crystallographic analysis at 2.6 Å resolution. OBPIIa is a monomeric protein that exhibits the classical lipocalin fold with a conserved eight-stranded β-barrel harboring a remarkably large hydrophobic pocket. Basic residues within the four loops that shape the entrance to this ligand-binding site evoke a positive electrostatic potential. Human OBPIIa shows distinct features compared with other mammalian OBPs, including a potentially reactive Cys side chain within its pocket similar to human tear lipocalin. PubMed: 25810031DOI: 10.1002/prot.24797 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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