We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

Cytochrome P450

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 11: Line 11:
== Structural highlights ==
== Structural highlights ==
-
The heme moiety iron is pentacoordinated with Cys as one ligand. The heme is stabilized by several side chains.
+
The heme moiety is stabilized by several side chains. The heme iron is pentacoordinated with Cys as one ligand.
</StructureSection>
</StructureSection>
== 3D Structures of Cytochrome P450 ==
== 3D Structures of Cytochrome P450 ==

Revision as of 10:00, 20 December 2015

Cytochrome P450 CypC2 with heme complex with warfarin (PDB entry 1og5)

Drag the structure with the mouse to rotate

3D Structures of Cytochrome P450

Updated on 20-December-2015

References

  1. Danielson PB. The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans. Curr Drug Metab. 2002 Dec;3(6):561-97. PMID:12369887

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools