1rlr: Difference between revisions
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[[Image:1rlr.jpg|left|200px]] | [[Image:1rlr.jpg|left|200px]] | ||
'''STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1''' | {{Structure | ||
|PDB= 1rlr |SIZE=350|CAPTION= <scene name='initialview01'>1rlr</scene>, resolution 2.5Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RLR is a [ | 1RLR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLR OCA]. | ||
==Reference== | ==Reference== | ||
Structure of ribonucleotide reductase protein R1., Uhlin U, Eklund H, Nature. 1994 Aug 18;370(6490):533-9. PMID:[http:// | Structure of ribonucleotide reductase protein R1., Uhlin U, Eklund H, Nature. 1994 Aug 18;370(6490):533-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8052308 8052308] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Ribonucleoside-diphosphate reductase]] | [[Category: Ribonucleoside-diphosphate reductase]] | ||
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[[Category: reductase (acting on ch2)]] | [[Category: reductase (acting on ch2)]] | ||
''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 13:53:19 2008'' | ||
Revision as of 11:53, 20 March 2008
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| 1rlr, resolution 2.5Å | |||||||||||||
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| Activity: | Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1
Overview
Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribonucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteins. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl end in a flexible arm. The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction.
About this Structure
1RLR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of ribonucleotide reductase protein R1., Uhlin U, Eklund H, Nature. 1994 Aug 18;370(6490):533-9. PMID:8052308
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