A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for deacylation

Summary for 4RVA

DescriptorBeta-lactamase TEM, BICARBONATE ION (3 entities in total)
Functional Keywordsglobular, beta-lactamase, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains1
Total molecular weight28957.93
Stojanoski, V.,Chow, D.-C.,Hu, L.,Sankaran, B.,Gilbert, H.,Prasad, B.V.V.,Palzkill, T. (deposition date: 2014-11-25, release date: 2015-03-04, Last modification date: 2015-05-06)
Primary citation
Stojanoski, V.,Chow, D.C.,Hu, L.,Sankaran, B.,Gilbert, H.F.,Prasad, B.V.,Palzkill, T.
A Triple Mutant in the Omega-loop of TEM-1 beta-Lactamase Changes the Substrate Profile via a Large Conformational Change and an Altered General Base for Catalysis.
J.Biol.Chem., 290:10382-10394, 2015
PubMed: 25713062 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M114.633438
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.19330 0.9% 1.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-10-21