Sandbox GGC8

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== Structural highlights ==
== Structural highlights ==
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<scene name='78/781194/92-63/2'>Proximal His87 and the distal His 58</scene> The α chain heme pocket with the relative orientation of the proximal Hisα87 and the distal Hisα58.proximal Hisα87(F8) is closer to the heme Fe atom by 0.10 Å more in the T-state compare to the R-state.<ref>doi: 10.1074/jbc.M109.066027</ref>
 
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<scene name='78/781194/87_-58_his/5'>Proximal His87 and the distal His 58</scene> The α chain heme pocket with the relative orientation of the proximal Hisα87 and the distal Hisα58.proximal Hisα87(F8) is closer to the heme Fe atom by 0.10 Å more in the T-state compare to the R-state.<ref>doi: 10.1074/jbc.M109.066027</ref>
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<scene name='78/781194/Hemoglobin/1'>This scene show the structure of the full hemoglobin </scene>
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<scene name='78/781194/92-63/3'>Proximal 92 His and distal 63 His </scene>) The β chain heme pocket with the proximal Hisβ92(F8) and the distal Hisβ63(E7). In the R-state the proximal Hisβ92(F8) reorients itself to a more symmetric position relative to the heme molecule. In the T-state, the distal histidine E7 residue is positioned such that it partially blocks the oxygen-binding site. During the R → T transition, Hisβ63(E7) aligns itself with the heme Fe, and the Fe-His distances increase by a small but detectable amount<ref>doi: 10.1074/jbc.M109.066027</ref>
<scene name='78/781194/92-63/3'>Proximal 92 His and distal 63 His </scene>) The β chain heme pocket with the proximal Hisβ92(F8) and the distal Hisβ63(E7). In the R-state the proximal Hisβ92(F8) reorients itself to a more symmetric position relative to the heme molecule. In the T-state, the distal histidine E7 residue is positioned such that it partially blocks the oxygen-binding site. During the R → T transition, Hisβ63(E7) aligns itself with the heme Fe, and the Fe-His distances increase by a small but detectable amount<ref>doi: 10.1074/jbc.M109.066027</ref>

Revision as of 04:15, 20 November 2019

Hemoglobin A

Caption for this structure

Drag the structure with the mouse to rotate

References

Crystal structure of Lysβ182-Lysβ282 crosslinked hemoglobin: A possible allosteric intermediate1 https://www.sciencedirect.com/science/article/pii/S0022283600935253?via%3Dihub#FIG4

  1. ↑ doi: https://dx.doi.org/10.1007/s10533-009-9387-8
  2. ↑ Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH. Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation. J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990 doi:10.1074/jbc.M109.066027
  3. ↑ Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH. Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation. J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990 doi:10.1074/jbc.M109.066027
  4. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  5. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

https://www.verywellhealth.com/importance-of-hemoglobin-2249107

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