3rgk: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rgk RCSB], [http://www.ebi.ac.uk/pdbsum/3rgk PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rgk RCSB], [http://www.ebi.ac.uk/pdbsum/3rgk PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/MYG_HUMAN MYG_HUMAN]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 09:12, 25 December 2014

Crystal Structure of Human Myoglobin Mutant K45RCrystal Structure of Human Myoglobin Mutant K45R

Structural highlights

3rgk is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2mm1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:MB (Homo sapiens)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[MYG_HUMAN] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

Publication Abstract from PubMed

We have grown crystals in trigonal space group P3(2)21 of a mutant human myoglobin, aquomet form, in which lysine at position 45 has been replaced by arginine and cysteine at position 110 has been replaced by alanine. Suitable crystals of native recombinant human myoglobin have not been obtained. We have used the molecular replacement method to determine the X-ray crystal structure of the mutant at 2.8 A resolution. At the present stage of refinement, the crystallographic R-value for the model, with tightly restrained stereochemistry, is 0.158 for 5.0 to 2.8 A data. As expected, the overall structure is quite similar to the sperm whale myoglobin structure. Arginine 45 adopts a well-ordered conformation similar to that found in aquomet sperm whale myoglobin.

X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution.,Hubbard SR, Hendrickson WA, Lambright DG, Boxer SG J Mol Biol. 1990 May 20;213(2):215-8. PMID:2342104[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Hubbard SR, Hendrickson WA, Lambright DG, Boxer SG. X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution. J Mol Biol. 1990 May 20;213(2):215-8. PMID:2342104

3rgk, resolution 1.65Å

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