1BH5

HUMAN GLYOXALASE I Q33E, E172Q DOUBLE MUTANT

Summary for 1BH5

DescriptorLACTOYLGLUTATHIONE LYASE, ZINC ION, S-HEXYLGLUTATHIONE, ... (4 entities in total)
Functional Keywordslyase, lactoylglutathione lyase, glyoxalase i
Biological sourceHomo sapiens (human)
Total number of polymer chains4
Total molecular weight84521.68
Authors
Cameron, A.D.,Jones, T.A. (deposition date: 1998-06-13, release date: 1998-11-04, Last modification date: 2018-03-14)
Primary citation
Ridderstrom, M.,Cameron, A.D.,Jones, T.A.,Mannervik, B.
Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I.
J.Biol.Chem., 273:21623-21628, 1998
PubMed: 9705294 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.273.34.21623
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers40.3%4.0%3.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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Molmil generated image of 1bh5
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More Biological unit images

Molmil generated image of 1bh5
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Molmil generated image of 1bh5
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(*)In the case of coarse surface representation, the asymmetric unit is shown as red ribbon representation.
Coordinate files for Biological unit (1bh5.pdb1.gz [66.44 KB])
Coordinate files for Biological unit (1bh5.pdb2.gz [65.73 KB])