1ABW
DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)
Summary for 1ABW
| Entry DOI | 10.2210/pdb1abw/pdb |
| Descriptor | HEMOGLOBIN-BASED BLOOD SUBSTITUTE, METHIONINE, LEUCINE, ... (6 entities in total) |
| Functional Keywords | heme, oxygen transport, respiratory protein, erythrocyte |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 65273.25 |
| Authors | Kundrot, C.E.,Kroeger, K.S. (deposition date: 1997-01-29, release date: 1998-06-17, Last modification date: 2024-05-22) |
| Primary citation | Kroeger, K.S.,Kundrot, C.E. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Structure, 5:227-237, 1997 Cited by PubMed Abstract: . Potential blood substitutes can be based on hemoglobin. Two problems must be overcome with acellular hemoglobin-based blood substitutes, however: the oxygen affinity of purified human hemoglobin is too high for it to deliver oxygen to tissues, and hemoglobin tetramers dissociate into alphabeta dimers that can cause kidney damage. A modified form of hemoglobin, rHb 1.1, has reduced oxygen affinity as the result of an Asnbeta 108-->Lys mutation, and dimerization is prevented by the insertion of a glycine residue between the sequences of the normal alpha chains to produce one covalently continuous di-alpha-chain. Determination of the structure of rHb 1.1 would provide structure-based explanations for the altered properties of rHb 1.1. PubMed: 9032082DOI: 10.1016/S0969-2126(97)00181-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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