4CK4
Ovine beta-Lactoglobulin at Atomic Resolution
Summary for 4CK4
| Entry DOI | 10.2210/pdb4ck4/pdb |
| Descriptor | BETA_LACTOGLOBULIN-1/B, SULFATE ION, AMMONIUM ION, ... (7 entities in total) |
| Functional Keywords | transport protein, ovine-lactoglobulin, high resolution |
| Biological source | OVIS ARIES (SHEEP) |
| Cellular location | Secreted: P67976 |
| Total number of polymer chains | 2 |
| Total formula weight | 37263.47 |
| Authors | Kontopidis, G.,Nordle, A.,Sawyer, L. (deposition date: 2013-12-27, release date: 2014-10-08, Last modification date: 2024-11-13) |
| Primary citation | Kontopidis, G.,Nordle Gilliver, A.,Sawyer, L. Ovine Beta-Lactoglobulin at Atomic Resolution Acta Crystallogr.,Sect.F, 70:1498-, 2014 Cited by PubMed Abstract: The crystal structure of the triclinic form of the milk protein β-lactoglobulin from sheep (Ovis aries) at 1.1 Å resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure. PubMed: 25372816DOI: 10.1107/S2053230X14020950 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.12 Å) |
Structure validation
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