1qks
From Proteopedia
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, resolution 1.28Å | |||||||
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Sites: | , , and | ||||||
Ligands: | , , , | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FORM
Overview
Cytochrome cd1-nitrite reductase is a bifunctional enzyme that catalyzes the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of oxygen to water. The 1.55 A crystal structure of the dimeric enzyme from Thiosphaera pantotropha is reported here. The protein was sequenced from the X-ray structure. Each subunit contains a covalent c heme with two axial His ligands (His-17, His-69) and a unique noncovalent d1 heme ligated by Tyr-25 and His-200. The d1 heme is the mononuclear iron center where both oxygen and nitrite reduction take place. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
About this Structure
1QKS is a Single protein structure of sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA.
Reference
The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1., Fulop V, Moir JW, Ferguson SJ, Hajdu J, Cell. 1995 May 5;81(3):369-77. PMID:7736589
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