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3hen
From Proteopedia
(Difference between revisions)
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| + | [[Image:3hen.jpg|left|200px]] | ||
| - | The | + | <!-- |
| + | The line below this paragraph, containing "STRUCTURE_3hen", creates the "Structure Box" on the page. | ||
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| + | {{STRUCTURE_3hen| PDB=3hen | SCENE= }} | ||
| - | + | ===Ferric Horse Heart Myoglobin; H64V/V67R Mutant=== | |
| - | Description: Ferric Horse Heart Myoglobin; H64V/V67R Mutant | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | <!-- |
| + | The line below this paragraph, {{ABSTRACT_PUBMED_19924902}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 19924902 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_19924902}} | ||
| + | |||
| + | ==About this Structure== | ||
| + | 3HEN is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HEN OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | <ref group="xtra">PMID:19924902</ref><references group="xtra"/> | ||
| + | [[Category: Equus caballus]] | ||
| + | [[Category: Richter-Addo, G B.]] | ||
| + | [[Category: Thomas, L M.]] | ||
| + | [[Category: Yi, J.]] | ||
| + | [[Category: Ferric myoglobin]] | ||
| + | [[Category: H64v/v67r mutant]] | ||
| + | [[Category: Heme]] | ||
| + | [[Category: Horse heart]] | ||
| + | [[Category: Iron]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Muscle protein]] | ||
| + | [[Category: Oxygen transport]] | ||
| + | [[Category: Transport]] | ||
| + | |||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 30 14:25:20 2009'' | ||
Revision as of 12:25, 30 December 2009
Ferric Horse Heart Myoglobin; H64V/V67R Mutant
Template:ABSTRACT PUBMED 19924902
About this Structure
3HEN is a 1 chain structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
- Yi J, Heinecke J, Tan H, Ford PC, Richter-Addo GB. The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron. J Am Chem Soc. 2009 Dec 23;131(50):18119-28. PMID:19924902 doi:10.1021/ja904726q
Page seeded by OCA on Wed Dec 30 14:25:20 2009
