2W6W
Crystal structure of recombinant Sperm Whale Myoglobin under 1atm of Xenon
Summary for 2W6W
| Entry DOI | 10.2210/pdb2w6w/pdb |
| Related | 101M 102M 103M 104M 105M 106M 107M 108M 109M 110M 111M 112M 1A6G 1A6K 1A6M 1A6N 1ABS 1AJG 1AJH 1BVC 1BVD 1BZ6 1BZP 1BZR 1CH1 1CH2 1CH3 1CH5 1CH7 1CH9 1CIK 1CIO 1CO8 1CO9 1CP0 1CP5 1CPW 1CQ2 1DO1 1DO3 1DO4 1DO7 1DTI 1DTM 1DUK 1DUO 1DXC 1DXD 1EBC 1F63 1F65 1F6H 1FCS 1H1X 1HJT 1IOP 1IRC 1J3F 1J52 1JDO 1JP6 1JP8 1JP9 1JPB 1JW8 1L2K 1LTW 1LUE 1MBC 1MBD 1MBI 1MBN 1MBO 1MCY 1MGN 1MLF 1MLG 1MLH 1MLJ 1MLK 1MLL 1MLM 1MLN 1MLO 1MLQ 1MLR 1MLS 1MLU 1MOA 1MOB 1MOC 1MOD 1MTI 1MTJ 1MTK 1MYF 1MYM 1MYZ 1MZ0 1N9F 1N9H 1N9I 1N9X 1NAZ 1O16 1OBM 1OFJ 1OFK 1SPE 1SWM 1TES 1U7R 1U7S 1UFJ 1UFP 1VXA 1VXB 1VXC 1VXD 1VXE 1VXF 1VXG 1VXH 1WVP 1YOG 1YOH 1YOI 2BLH 2BLI 2BLJ 2BW9 2BWH 2CMM 2D6C 2EVP 2G0R 2G0S 2G0V 2G0X 2G0Z 2G10 2G11 2G12 2G14 2JHO 2MB5 2MBW 2MGA 2MGB 2MGC 2MGD 2MGE 2MGF 2MGG 2MGH 2MGI 2MGJ 2MGK 2MGL 2MGM 2MYA 2MYB 2MYC 2MYD 2MYE 2SPL 2SPM 2SPN 2SPO 2W6V 2W6X 2W6Y 2W72 4MBN 5MBN |
| Descriptor | MYOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, XENON, ... (6 entities in total) |
| Functional Keywords | hydrophobic cavities, oxygen storage, oxygen transport, xenon docking site, iron, heme, transport, metal-binding, muscle protein |
| Biological source | PHYSETER CATODON (SPERM WHALE) |
| Total number of polymer chains | 1 |
| Total formula weight | 18984.15 |
| Authors | Miele, A.E.,Draghi, F.,Renzi, F.,Sciara, G.,Johnson, K.A.,Vallone, B.,Brunori, M.,Savino, C. (deposition date: 2008-12-19, release date: 2009-04-28, Last modification date: 2023-12-13) |
| 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 (1.99 Å) |
Structure validation
Download full validation report
