1y8h
From Proteopedia
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| - | [[Image:1y8h.gif|left|200px]] | + | [[Image:1y8h.gif|left|200px]] |
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| - | '''HORSE METHEMOGLOBIN LOW SALT, PH 7.0''' | + | {{Structure |
| + | |PDB= 1y8h |SIZE=350|CAPTION= <scene name='initialview01'>1y8h</scene>, resolution 3.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HORSE METHEMOGLOBIN LOW SALT, PH 7.0''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Y8H is a [ | + | 1Y8H is a [[Protein complex]] structure of sequences 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=1Y8H OCA]. |
==Reference== | ==Reference== | ||
| - | A new relaxed state in horse methemoglobin characterized by crystallographic studies., Sankaranarayanan R, Biswal BK, Vijayan M, Proteins. 2005 Aug 15;60(3):547-51. PMID:[http:// | + | A new relaxed state in horse methemoglobin characterized by crystallographic studies., Sankaranarayanan R, Biswal BK, Vijayan M, Proteins. 2005 Aug 15;60(3):547-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15887226 15887226] |
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: quarternary association]] | [[Category: quarternary association]] | ||
| - | ''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 15:19:46 2008'' |
Revision as of 13:19, 20 March 2008
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| , resolution 3.10Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HORSE METHEMOGLOBIN LOW SALT, PH 7.0
Overview
A new relaxed state has been characterized in the crystals of horse methemoglobin grown at neutral pH at low ionic concentration and their low humidity variants. The crystals provide an example for improvement in X-ray diffraction quality with reduced solvent content. Only the classical R state has been so far observed in liganded horse hemoglobin. The state characterized in the present study lies in between the R state and the R2 state characterized earlier in liganded human hemoglobin. The results presented here, along with those of earlier studies, suggest that relaxed and tense hemoglobin can access ensembles of states.
About this Structure
1Y8H is a Protein complex structure of sequences from Equus caballus. Full crystallographic information is available from OCA.
Reference
A new relaxed state in horse methemoglobin characterized by crystallographic studies., Sankaranarayanan R, Biswal BK, Vijayan M, Proteins. 2005 Aug 15;60(3):547-51. PMID:15887226
Page seeded by OCA on Thu Mar 20 15:19:46 2008
