1UM2

Crystal Structure of the Vma1-Derived Endonuclease with the Ligated Extein Segment

Summary for 1UM2

Related1JVA
DescriptorENDONUCLEASE PI-SCEI, 21-mer from Vacuolar ATP synthase catalytic subunit A (3 entities in total)
Functional Keywordsprotein splicing, vma1-derived endonuclease, vde, intein, extein, thiazolidine, hydrolase
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationEndomembrane system  P17255 P17255
Total number of polymer chains4
Total molecular weight106390.38
Authors
Mizutani, R.,Anraku, Y.,Satow, Y. (deposition date: 2003-09-22, release date: 2004-09-22, Last modification date: 2017-08-23)
Primary citation
Mizutani, R.,Anraku, Y.,Satow, Y.
Protein splicing of yeast VMA1-derived endonuclease via thiazolidine intermediates.
J.Synchrotron Radiat., 11:109-112, 2004
PubMed: 14646148 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.9 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers497.6%10.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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More Biological unit images

Molmil generated image of 1um2
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Molmil generated image of 1um2
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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 (1um2.pdb2.gz [71.41 KB])
Coordinate files for Biological unit (1um2.pdb1.gz [71.2 KB])