1M40

ULTRA HIGH RESOLUTION CRYSTAL STRUCTURE OF TEM-1

Replaces:  1L7U

Summary for 1M40

DescriptorBETA-LACTAMASE TEM, PHOSPHATE ION, POTASSIUM ION, ... (5 entities in total)
Functional Keywordsbeta-lactamase, acylation mechanism, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains1
Total molecular weight29683.33
Authors
Minasov, G.,Wang, X.,Shoichet, B.K. (deposition date: 2002-07-01, release date: 2002-07-17, Last modification date: 2011-07-13)
Primary citation
Minasov, G.,Wang, X.,Shoichet, B.K.
An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation.
J.Am.Chem.Soc., 124:5333-5340, 2002
PubMed: 11996574 (PDB entries with the same primary citation)
DOI: 10.1021/ja0259640
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (0.85 Å)
NMR Information
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.117701.8%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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