3mba

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[[Image:3mba.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_3mba", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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{{STRUCTURE_3mba| PDB=3mba | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mba OCA], [http://www.ebi.ac.uk/pdbsum/3mba PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3mba RCSB]</span>
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'''APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION'''
'''APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION'''
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[[Category: Gatti, G.]]
[[Category: Gatti, G.]]
[[Category: Onesti, S.]]
[[Category: Onesti, S.]]
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[[Category: oxygen storage]]
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[[Category: Oxygen storage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:06:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:34:34 2008''
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Revision as of 19:06, 4 May 2008

Image:3mba.jpg

Template:STRUCTURE 3mba

APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION


Overview

The crystal structure of the ferric form of myoglobin from the mollusc Aplysia limacina has been refined at 1.6 A resolution, by restrained crystallographic refinement methods. The crystallographic R-factor is 0.19. The tertiary structure of the molecule conforms to the common globin fold, consisting of eight alpha-helices. The N-terminal helix A and helix G deviate significantly from linearity. The distal residue is recognized as Val63 (E7), which, however, does not contact the heme directly. Moreover the sixth (distal) co-ordination position of heme iron is not occupied by a water molecule at neutrality, i.e. below the acid-alkaline transition point of A. limacina myoglobin. The heme group sits in its crevice in the conventional orientation and no signs of heme isomerism are evident. The iron atom is 0.26 A out of the porphyrin plane, with a mean Fe-N (porphyrin) distance of 2.01 A. The co-ordination bond to the proximal histidine has a length of 2.05 A, and forms an angle of 4 degrees with the heme normal. A plane containing the imidazole ring of the proximal His intersects the heme at an angle of 29 degrees with the (porphyrin) 4N-2N direction. Inspection of the structure of pH 9.0 indicates that a hydroxyl ion is bound to the Fe sixth co-ordination position.

About this Structure

3MBA is a Single protein structure of sequence from Aplysia limacina. Full crystallographic information is available from OCA.

Reference

Aplysia limacina myoglobin. Crystallographic analysis at 1.6 A resolution., Bolognesi M, Onesti S, Gatti G, Coda A, Ascenzi P, Brunori M, J Mol Biol. 1989 Feb 5;205(3):529-44. PMID:2926816 Page seeded by OCA on Sun May 4 22:06:49 2008

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