Alpha Globin
(based on 1HHO.pdb1.gz)
Above, you should see the adult hemoglobin A (HbA) tetramer (2 alpha and 2 beta globins)depicted in cpk colors.
The two alpha globin monomers are shown in light pink colors and the two betaglobin molecules are shown in light blue.
The heme groups are highlighted in red in this model of HgA with the oxygen molecules that are attached being shown in green. Notice how they are carefully packed away.
Here the focus is on one alphaglobin molecule
In this model the alphaglobin molecule is represented with a light pink backbone. The key residues in binding with the hem group(off white) are shown in tan, the proximal histidine is shown in purple while the distal histidine is in firebrick red. If you look carefully you can see that the ferrous group is depicted in yellow.
This model shows the different amino acids that make up the alpha globin molecule. The heme group is depicted in lime green. Notice the purple distal and proximal histidines.
This alpha globin model shows the polar(hydrophilic)residues in magenta and the nonpolar(hydrophobic) residues in yellow. The heme group is depicted in lime green.
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Beta Globin
(based on 1HHO.pdb1.gz)
Above, you should see the adult hemoglobin A (HbA) tetramer (2 alpha and 2 beta globins)depicted in cpk colors.
Here the 141 residue alpha globin monomer is on the left, the 146 residue beta globin monomer is on the right.
Here you see just the betaglobin chain depicted with the heme group and associated oxygen highlighted in red and green respectively.
The beta chain is represented with a backbone showing the heme group(off white) with associated oxygen in green. The proximal histidine is in purple, while the distal histidine is shown in firebrick red. The otherimportant heme binding residues are shown in tan.
This model shows the different amino acids that make up the alpha globin molecule. The heme group is depicted in lime green. Notice the purple distal and proximal histidines.
This beta globin model shows the polar(hydrophilic)residues in magenta and the nonpolar(hydrophobic) residues in yellow. The heme group is depicted in lime green.
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Gamma Globin (based on 4MQJ.pdb)
Above, you should see the fetal hemoglobin F (HbF) tetramer (2 alpha and 2 gamma globins)depicted in cpk colors.
This model shows the two alpha globins in pink and the gamma globin monomers in khaki. The associated heme groups with each model are shown in red.
Backbone of entire human fetal hemoglobin with both alpha and gamma chains, also including heme groups. Alpha are red and green. Gamma is yellow and blue.
Here's the spacefill model of just one of gamma globins. The heme group is shown in red. It should be noted that like the beta globins, gamma globins have 146 residues.
The gamma chain is represented with a backbone showing the heme group(off white) with associated oxygen in green. The proximal histidine is in purple, while the distal histidine is shown in firebrick red. The other important heme binding residues are shown in tan.
This model shows the different amino acids that make up the gamma globin molecule. The heme group is depicted in lime green. Notice the purple distal and proximal histidines.
This gamma globin model shows the polar(hydrophilic)residues in magenta and the nonpolar(hydrophobic) residues in yellow. The heme group is depicted in lime green.
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