This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1qks
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1qks.jpg|left|200px]] | + | [[Image:1qks.jpg|left|200px]] |
| - | + | ||
| - | '''CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FORM''' | + | {{Structure |
| + | |PDB= 1qks |SIZE=350|CAPTION= <scene name='initialview01'>1qks</scene>, resolution 1.28Å | ||
| + | |SITE= <scene name='pdbsite=C1A:The+C+Haem+Is+The+Point+Of+Electron+Entry'>C1A</scene>, <scene name='pdbsite=C1B:The+C+Haem+Is+The+Point+Of+Electron+Entry'>C1B</scene>, <scene name='pdbsite=D1A:The+D1+Haem+Is+The+Site+Of+Catalytic+Acti'>D1A</scene> and <scene name='pdbsite=D1B:The+D1+Haem+Is+The+Site+Of+Catalytic+Acti'>D1B</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=DHE:HEME+D'>DHE</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FORM''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1QKS is a [ | + | 1QKS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7736589 7736589] |
[[Category: Paracoccus denitrificans]] | [[Category: Paracoccus denitrificans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: periplasmic]] | [[Category: periplasmic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:38:59 2008'' |
Revision as of 11:39, 20 March 2008
| |||||||
| , resolution 1.28Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , and | ||||||
| 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
Page seeded by OCA on Thu Mar 20 13:38:59 2008
Categories: Paracoccus denitrificans | Single protein | Fulop, V. | DHE | GOL | HEC | SO4 | Denitrification | Electron transport | Enzyme | Nitrite reductase | Oxidoreductase | Periplasmic
