3EU1
Crystal Structure determination of goat hemoglobin (Capra hircus) at 3 angstrom resolution
Summary for 3EU1
| Entry DOI | 10.2210/pdb3eu1/pdb |
| Related | 2qu0 2ri4 3cy5 3d1a 3d4x |
| Descriptor | Hemoglobin subunit alpha-1/2, Hemoglobin subunit beta-A, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | low oxygen affinity, capra hircus, hemoglobin, allosteric mechanism, 2, 3-diphospho glycerate, oxygen storage, oxygen transport |
| Biological source | Capra hircus (domestic goat, goats) More |
| Total number of polymer chains | 4 |
| Total formula weight | 64671.07 |
| Authors | Sathya Moorthy, P.,Neelagandan, K.,Balasubramanian, M.,Ponnuswamy, M.N. (deposition date: 2008-10-09, release date: 2009-11-10, Last modification date: 2023-11-01) |
| Primary citation | Sathya Moorthy, P.,Neelagandan, K.,Balasubramanian, M.,Ponnuswamy, M.N. Purification, crystallization and preliminary X-ray diffraction studies on goat (Capra hircus) hemoglobin - a low oxygen affinity species Protein Pept.Lett., 16:454-456, 2009 Cited by PubMed Abstract: Hemoglobin is a vital protein present in almost all higher species. It is a transport protein involved in carrying oxygen from lungs to tissues and carbon dioxide back to lungs by an intrinsically coordinated manner. Even though a good amount of work has been carried out in this direction there exists scarcity of structural insight on low oxygen affinity species. Attempts are being made to unravel the structural insight of this low oxygen affinity species. Goat blood plasma was collected, treated with EDTA to avoid blood clotting and purification was accomplished using DEAE-anion chromatographic column. The goat hemoglobin was crystallized using 50mM of phosphate buffer at pH 6.7 with 1M NaCl and PEG 3350 as precipitant by hanging drop vapor diffusion method. Crystals obtained are screened and suitable crystals are taken for data collection using mar345dtb as image plate detector system. Goat hemoglobin crystal diffracted up to 2.61 A resolution. Goat hemoglobin crystallizes in orthorhombic space group P212(1)2(1) as a whole biological molecule in the asymmetric unit with cell dimensions a=53.568A, b=67.365A, c=154.183A. PubMed: 19356147DOI: 10.2174/092986609787847992 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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