1Y8I
Horse methemoglobin low salt, PH 7.0 (98% relative humidity)
Summary for 1Y8I
| Entry DOI | 10.2210/pdb1y8i/pdb |
| Related | 1JY7 1LFQ 1Y8H 1Y8K |
| Descriptor | Hemoglobin alpha chains, Hemoglobin beta chain, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | aquo methemoglobin, quarternary association, allosteric transition, protein hydration, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Equus caballus (horse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 64807.06 |
| Authors | Sankaranarayanan, R.,Biswal, B.K.,Vijayan, M. (deposition date: 2004-12-13, release date: 2005-07-26, Last modification date: 2023-08-23) |
| Primary citation | Sankaranarayanan, R.,Biswal, B.K.,Vijayan, M. A new relaxed state in horse methemoglobin characterized by crystallographic studies. Proteins, 60:547-551, 2005 Cited by PubMed Abstract: A new relaxed state has been characterized in the crystals of horse methemoglobin grown at neutral pH at low ionic concentration and their low humidity variants. The crystals provide an example for improvement in X-ray diffraction quality with reduced solvent content. Only the classical R state has been so far observed in liganded horse hemoglobin. The state characterized in the present study lies in between the R state and the R2 state characterized earlier in liganded human hemoglobin. The results presented here, along with those of earlier studies, suggest that relaxed and tense hemoglobin can access ensembles of states. PubMed: 15887226DOI: 10.1002/prot.20510 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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