2aur: Difference between revisions
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[[Image:2aur.gif|left|200px]] | [[Image:2aur.gif|left|200px]] | ||
'''F97V (no ligand bound)''' | {{Structure | ||
|PDB= 2aur |SIZE=350|CAPTION= <scene name='initialview01'>2aur</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''F97V (no ligand bound)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2AUR is a [ | 2AUR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Scapharca_inaequivalvis Scapharca inaequivalvis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AUR OCA]. | ||
==Reference== | ==Reference== | ||
Residue F4 plays a key role in modulating oxygen affinity and cooperativity in Scapharca dimeric hemoglobin., Knapp JE, Bonham MA, Gibson QH, Nichols JC, Royer WE Jr, Biochemistry. 2005 Nov 8;44(44):14419-30. PMID:[http:// | Residue F4 plays a key role in modulating oxygen affinity and cooperativity in Scapharca dimeric hemoglobin., Knapp JE, Bonham MA, Gibson QH, Nichols JC, Royer WE Jr, Biochemistry. 2005 Nov 8;44(44):14419-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16262242 16262242] | ||
[[Category: Scapharca inaequivalvis]] | [[Category: Scapharca inaequivalvis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxygen transport]] | [[Category: oxygen 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 15:54:06 2008'' | ||
