1SPA

ROLE OF ASP222 IN THE CATALYTIC MECHANISM OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE: THE AMINO ACID RESIDUE WHICH ENHANCES THE FUNCTION OF THE ENZYME-BOUND COENZYME PYRIDOXAL 5'-PHOSPHATE

Summary for 1SPA

DescriptorASPARTATE AMINOTRANSFERASE, N-METHYL-4-DEOXY-4-AMINO-PYRIDOXAL-5-PHOSPHATE (3 entities in total)
Functional Keywordstransferase(aminotransferase)
Biological sourceEscherichia coli
Cellular locationCytoplasm P00509
Total number of polymer chains1
Total molecular weight43838.41
Authors
Hinoue, Y.,Yano, T.,Metzler, D.E.,Miyahara, I.,Hirotsu, K.,Kagamiyama, H. (deposition date: 1993-01-26, release date: 1993-10-31, Last modification date: 2017-11-29)
Primary citation
Yano, T.,Kuramitsu, S.,Tanase, S.,Morino, Y.,Kagamiyama, H.
Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.
Biochemistry, 31:5878-5887, 1992
PubMed: 1610831 (PDB entries with the same primary citation)
DOI: 10.1021/bi00140a025
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2 Å)
?

Structure validation

ClashscoreRamachandran outliersSidechain outliers14 1.0% 16.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
171916
PDB entries from 2020-12-02