1TG9

Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

Summary for 1TG9

Related1T9N 1TB0 1TBT 1TE3 1TEQ 1TEU 1TG3 1TH9 1THK
DescriptorCarbonic anhydrase II, ZINC ION (3 entities in total)
Functional Keywordsproton shuttle carbonic anhydrase metalloenzyme, lyase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm  P00918
Total number of polymer chains1
Total molecular weight29378.51
Authors
Fisher, Z.,Hernandez Prada, J.A.,Tu, C.K.,Duda, D.,Yoshioka, C.,An, H.,Govindasamy, L.,Silverman, D.N.,McKenna, R. (deposition date: 2004-05-28, release date: 2005-01-25, Last modification date: 2017-10-11)
Primary citation
Fisher, Z.,Hernandez Prada, J.A.,Tu, C.K.,Duda, D.,Yoshioka, C.,An, H.,Govindasamy, L.,Silverman, D.N.,McKenna, R.
Structural and Kinetic Characterization of Active-Site Histidine as a Proton Shuttle in Catalysis by Human Carbonic Anhydrase II
Biochemistry, 44:1097-1105, 2005
PubMed: 15667203 (PDB entries with the same primary citation)
DOI: 10.1021/bi0480279
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.9 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.217700.9%1.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 1tg9
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Molmil generated image of 1tg9
rotated about x axis by 90°
Molmil generated image of 1tg9
rotated about y axis by 90°