3X35: Crystal structure of the reduced form of the solubilized domain of porcine cytochrome b5 in form 2 crystal

Mammalian microsomal cytochrome b5 has multiple electron-transfer partners that function in various electron-transfer reactions. Four crystal structures of the solubilized haem-binding domain of cytochrome b5 from porcine liver were determined at sub-angstrom resolution (0.76-0.95 A) in two crystal forms for both the oxidized and reduced states. The high-resolution structures clearly displayed the electron density of H atoms in some amino-acid residues. Unrestrained refinement of bond lengths revealed that the protonation states of the haem propionate group may be involved in regulation of the haem redox properties. The haem Fe coordination geometry did not show significant differences between the oxidized and reduced structures. However, structural differences between the oxidized and reduced states were observed in the hydrogen-bond network around the axial ligand His68. The hydrogen-bond network could be involved in regulating the redox states of the haem group.
PDB ID: 3X35Download
MMDB ID: 130796
PDB Deposition Date: 2015/1/14
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 0.95  Å
Source Organism:
Similar Structures:
Biological Unit for 3X35: monomeric; determined by author and by software (PISA)
Molecular Components in 3X35
Label Count Molecule
Protein (1 molecule)
Cytochrome B5(Gene symbol: CYB5A)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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