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3RGK

Crystal Structure of Human Myoglobin Mutant K45R

Replaces:  2MM1
Summary for 3RGK
Entry DOI10.2210/pdb3rgk/pdb
DescriptorMyoglobin, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
Functional Keywordsheme, oxygen transport
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight17984.28
Authors
Hubbard, S.R. (deposition date: 2011-04-08, release date: 2011-04-27, Last modification date: 2023-09-13)
Primary citationHubbard, S.R.,Lambright, S.G.,Boxer, S.G.,Hendrickson, W.A.
X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution
J.Mol.Biol., 20:215-218, 1990
Cited by
PubMed Abstract: 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crystals in trigonal space group P3(2)21 of a mutant human myoglobin, aquomet form, in which lysine at position 45 has been replaced by arginine and cysteine at position 110 has been replaced by alanine.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.
PubMed: 2342104
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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