1hjt | pdb_00001hjt

SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)

spinqualitylabelsall models 1hjt, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1hjt is a 1 chain structure with sequence from Physeter catodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM, NO, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of the ferrous nitric oxide form of native sperm whale myoglobin has been determined by X-ray crystallography to 1.7 angstroms resolution. The nitric oxide ligand is bent with respect to the heme plane: the Fe-N-O angle is 112 degrees. This angle is smaller than those observed in model compounds and in lupin leghemoglobin. The exact angle appears to be influenced by the strength of the proximal bond and hydrogen bonding interactions between the distal histidine and the bound ligand. Specifically, the N(epsilon) atom of histidine64 is located 2.8 angstroms away from the nitrogen atom of the bound ligand, implying electrostatic stabilization of the FeNO complex. This interpretation is supported by mutagenesis studies. When histidine64 is replaced with apolar amino acids, the rate of nitric oxide dissociation from myoglobin increases tenfold. Nitric oxide myoglobin: crystal structure and analysis of ligand geometry.,Brucker EA, Olson JS, Ikeda-Saito M, Phillips GN Jr Proteins. 1998 Mar 1;30(4):352-6. PMID:9533619 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myoglobin

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