1qks
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1qks |SIZE=350|CAPTION= <scene name='initialview01'>1qks</scene>, resolution 1.28Å | |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> | |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= | + | |LIGAND= <scene name='pdbligand=DHE:HEME+D'>DHE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qks OCA], [http://www.ebi.ac.uk/pdbsum/1qks PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qks RCSB]</span> | ||
}} | }} | ||
| Line 23: | Line 26: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
| - | [[Category: DHE]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: HEC]] | ||
| - | [[Category: SO4]] | ||
[[Category: denitrification]] | [[Category: denitrification]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| Line 34: | Line 33: | ||
[[Category: periplasmic]] | [[Category: periplasmic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:07 2008'' |
Revision as of 20:15, 30 March 2008
| |||||||
| , resolution 1.28Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
Page seeded by OCA on Sun Mar 30 23:15:07 2008
