1QHP

FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE COMPLEX

Summary for 1QHP

Related1QHO
Related PRD IDPRD_900001
DescriptorALPHA-AMYLASE, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
Functional Keywordsamylase, glycoside hydrolase, starch degradation, hydrolase
Biological sourceGeobacillus stearothermophilus
Total number of polymer chains1
Total molecular weight76800.3
Authors
Dauter, Z.,Dauter, M.,Brzozowski, A.M.,Christensen, S.,Borchert, T.V.,Beier, L.,Wilson, K.S.,Davies, G.J. (deposition date: 1999-05-25, release date: 2000-05-31, Last modification date: 2020-07-29)
Primary citation
Dauter, Z.,Dauter, M.,Brzozowski, A.M.,Christensen, S.,Borchert, T.V.,Beier, L.,Wilson, K.S.,Davies, G.J.
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
Biochemistry, 38:8385-8392, 1999
PubMed: 10387084 (PDB entries with the same primary citation)
DOI: 10.1021/bi990256l
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.7 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers2 0.1% 0.9% 0.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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171916
PDB entries from 2020-12-02