1TB0

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

Summary for 1TB0

Related1T9N 1TBT 1TE3 1TEQ 1TEU
DescriptorCarbonic anhydrase II, ZINC ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsproton shuttle carbonic anhydrase metalloenzyme, lyase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm  P00918
Total number of polymer chains1
Total molecular weight29389.92
Authors
Fisher, Z.,Hernandez Prada, J.A.,Tu, C.,Duda, D.,Yoshioka, C.,An, H.,Govindasamy, L.,Silverman, D.N.,McKenna, R. (deposition date: 2004-05-19, release date: 2005-01-25, Last modification date: 2017-10-11)
Primary citation
Fisher, Z.,Hernandez Prada, J.A.,Tu, C.,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 (2 Å)
?

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.205304.5%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 1tb0
no rotation
Molmil generated image of 1tb0
rotated about x axis by 90°
Molmil generated image of 1tb0
rotated about y axis by 90°