1cot
From Proteopedia
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| - | [[Image:1cot.jpg|left|200px]] | + | [[Image:1cot.jpg|left|200px]] |
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| - | '''X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1cot |SIZE=350|CAPTION= <scene name='initialview01'>1cot</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1COT is a [ | + | 1COT 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=1COT OCA]. |
==Reference== | ==Reference== | ||
| - | X-Ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7-A resolution., Benning MM, Meyer TE, Holden HM, Arch Biochem Biophys. 1994 May 1;310(2):460-6. PMID:[http:// | + | X-Ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7-A resolution., Benning MM, Meyer TE, Holden HM, Arch Biochem Biophys. 1994 May 1;310(2):460-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8179333 8179333] |
[[Category: Paracoccus denitrificans]] | [[Category: Paracoccus denitrificans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''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 10:27:03 2008'' |
Revision as of 08:27, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION
Overview
The cytochrome c2 (formerly c550) isolated from Paracoccus denitrificans is one of the larger bacterial c-type proteins examined thus far. The molecular structure of this cytochrome has been redetermined and refined to 1.7-A resolution with a crystallographic R-factor of 17.5% for all measured X-ray data. Like other, smaller c-type cytochromes, the molecule consists of five alpha-helices that wrap around the heme group. In addition, this bacterial cytochrome contains two strands of anti-parallel beta-sheet, five Type I turns, and three Type II turns. The present model differs from the originally determined structure in several regions including the N-terminus, the loop delineated by Asp 25 to Lys 31, the region defined by Trp 86 to Val 88, and the C-terminus. A total of 103 water molecules has been positioned into the electron density map. Six of these waters are directly involved in heme binding.
About this Structure
1COT is a Single protein structure of sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA.
Reference
X-Ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7-A resolution., Benning MM, Meyer TE, Holden HM, Arch Biochem Biophys. 1994 May 1;310(2):460-6. PMID:8179333
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