1cqx: Difference between revisions
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|PDB= 1cqx |SIZE=350|CAPTION= <scene name='initialview01'>1cqx</scene>, resolution 1.75Å | |PDB= 1cqx |SIZE=350|CAPTION= <scene name='initialview01'>1cqx</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=DGG:1-[GLYCEROLYLPHOSPHONYL]-2-[8-(2-HEXYL-CYCLOPROPYL)-OCTANAL-1-YL]-3-[HEXADECANAL-1-YL]-GLYCEROL'>DGG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqx OCA], [http://www.ebi.ac.uk/pdbsum/1cqx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cqx RCSB]</span> | |||
}} | }} | ||
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[[Category: Friedrich, B.]] | [[Category: Friedrich, B.]] | ||
[[Category: Siddiqui, R A.]] | [[Category: Siddiqui, R A.]] | ||
[[Category: globin fold]] | [[Category: globin fold]] | ||
[[Category: helix-flanked five-stranded parallel beta sheet]] | [[Category: helix-flanked five-stranded parallel beta sheet]] | ||
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[[Category: six-stranded antiparallel beta sheet]] | [[Category: six-stranded antiparallel beta sheet]] | ||
''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 19:26:54 2008'' | ||
Revision as of 19:26, 30 March 2008
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| , resolution 1.75Å | |||||||
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| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution
OverviewOverview
The molecular structure of the flavohemoglobin from Alcaligenes eutrophus has been determined to a resolution of 1.75 A and refined to an R-factor of 19.6%. The protein comprises two fused modules: a heme binding module, which belongs to the globin family, and an FAD binding oxidoreductase module, which adopts a fold like ferredoxin reductase. The most striking deviation of the bacterial globin structure from those of other species is the movement of helix E in a way to provide more space in the vicinity of the distal heme binding site. A comparison with other members of the ferredoxin reductase family shows similar tertiary structures for the individual FAD and NAD binding domains but largely different interdomain orientations. The heme and FAD molecules approach each other to a minimal distance of 6.3 A and adopt an interplanar angle of 80 degrees. The electron transfer from FAD to heme occurs in a predominantly polar environment and may occur directly or be mediated by a water molecule.
About this StructureAbout this Structure
1CQX is a Single protein structure of sequence from Cupriavidus necator. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution., Ermler U, Siddiqui RA, Cramm R, Friedrich B, EMBO J. 1995 Dec 15;14(24):6067-77. PMID:8557026
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