2W72
DEOXYGENATED STRUCTURE OF A DISTAL SITE HEMOGLOBIN MUTANT PLUS XE
Summary for 2W72
| Entry DOI | 10.2210/pdb2w72/pdb |
| Related | 1A00 1A01 1A0U 1A0Z 1A3N 1A3O 1A9W 1ABW 1ABY 1AJ9 1B86 1BAB 1BBB 1BIJ 1BUW 1BZ0 1BZ1 1BZZ 1C7B 1C7C 1C7D 1CBL 1CBM 1CH4 1CLS 1CMY 1COH 1DKE 1DXT 1DXU 1DXV 1FDH 1FN3 1G9V 1GBU 1GBV 1GLI 1GZX 1HAB 1HAC 1HBA 1HBB 1HBS 1HCO 1HDB 1HGA 1HGB 1HGC 1HHO 1IRD 1J3Y 1J3Z 1J40 1J41 1J7S 1J7W 1J7Y 1JY7 1K0Y 1K1K 1KD2 1LFL 1LFQ 1LFT 1LFV 1LFY 1LFZ 1LJW 1M9P 1MKO 1NEJ 1NIH 1NQP 1O1I 1O1J 1O1K 1O1L 1O1M 1O1N 1O1O 1O1P 1QI8 1QSH 1QSI 1QXD 1QXE 1R1X 1R1Y 1RPS 1RQ3 1RQ4 1RQA 1RVW 1SDK 1SDL 1SHR 1SI4 1THB 1UIW 1VWT 1XXT 1XY0 1XYE 1XZ2 1XZ4 1XZ5 1XZ7 1XZU 1XZV 1Y01 1Y09 1Y0A 1Y0C 1Y0D 1Y0T 1Y0W 1Y22 1Y2Z 1Y31 1Y35 1Y45 1Y46 1Y4B 1Y4F 1Y4G 1Y4P 1Y4Q 1Y4R 1Y4V 1Y5F 1Y5J 1Y5K 1Y7C 1Y7D 1Y7G 1Y7Z 1Y83 1Y85 1Y8W 1YDZ 1YE0 1YE1 1YE2 1YEN 1YEO 1YEQ 1YEU 1YEV 1YFF 1YG5 1YGD 1YGF 1YH9 1YHE 1YHR 1YIE 1YIH 1YVQ 1YVT 1YZI 1Z8U 2D5Z 2D60 2DN1 2DN2 2DN3 2HBC 2HBD 2HBE 2HBF 2HBS 2HCO 2HHD 2HHE 2W6V 2W6W 2W6X 2W6Y 4HHB 6HBW |
| Descriptor | HUMAN HEMOGLOBIN A, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (9 entities in total) |
| Functional Keywords | iron, heme, glycation, transport, acetylation, phosphoprotein, packing defects, disease mutation, distal site point mutation, oxygen transport, hydrophobic cavities, polymorphism, glycoprotein, metal-binding |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 4 |
| Total formula weight | 67753.41 |
| Authors | Miele, A.E.,Draghi, F.,Sciara, G.,Johnson, K.A.,Renzi, F.,Vallone, B.,Brunori, M.,Savino, C. (deposition date: 2008-12-19, release date: 2009-04-28, Last modification date: 2024-02-07) |
| Primary citation | Savino, C.,Miele, A.E.,Draghi, F.,Johnson, K.A.,Sciara, G.,Brunori, M.,Vallone, B. Pattern of Cavities in Globins: The Case of Human Hemoglobin. Biopolymers, 91:1097-, 2009 Cited by PubMed Abstract: Our aim is to shed light on the conservation of potential ligand docking sites that play an important role in ligand dynamics of globins by using the technique of filling internal cavities naturally present in hemoglobin and myoglobin with xenon atoms. In particular, we present the high resolution structures of the Xe-adduct of deoxygenated wild type human hemoglobin and a quadruple mutant (L(B10)Y and H(E7)Q in alpha and beta chains). For the sake of comparison we also determined under the same experimental conditions the xenon complex of wild type sperm whale myoglobin. The analysis revealed that the number and position of Xe binding cavities are different in the alpha and beta subunits, the latter being more similar to myoglobin. Notably, no proximal Xe docking site was detected in hemoglobin, at variance with myoglobin. The pattern of internal cavities accessibility and affinity for xenon suggests a different role for the dynamics of ligand migration in the two types of hemoglobin chains as compared to myoglobin. The number and position of hydrophobic cavities in hemoglobin are briefly discussed also in comparison with the data available for other members of the globin superfamily. PubMed: 19365817DOI: 10.1002/BIP.21201 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.07 Å) |
Structure validation
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