1kfr

Structural plasticity in the eight-helix fold of a trematode hemoglobinStructural plasticity in the eight-helix fold of a trematode hemoglobin

Structural highlights 1kfr is a 1 chain structure with sequence from Paramphistomum epiclitum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Related: 1h97 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [GLB_PAREP] Oxygen binding protein. 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 three-dimensional structure of recombinant haemoglobin from the trematode Paramphistomum epiclitum, displaying the highest oxygen affinity so far observed for (non)vertebrate haemoglobins, has previously been determined at 1.17 A resolution (orthorhombic space group P2(1)2(1)2(1)). In the present communication, the three-dimensional structure of wild-type P. epiclitum haemoglobin is reported at 1.85 A resolution in a monoclinic crystal form (R factor = 16.1%, R(free) = 22.0%). Comparison of P. epiclitum (recombinant versus wild-type ferric Hb) structures in the two crystal forms shows structural differences in the haem proximal and distal sites which have not been reported for other known haemoglobin structures previously. Structural plasticity in the eight-helix fold of a trematode haemoglobin.,Milani M, Pesce A, Dewilde S, Ascenzi P, Moens L, Bolognesi M Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):719-22. Epub 2002, Mar 22. PMID:11914507 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemoglobin 3D structures

spinqualitylabelsall models 1kfr, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image