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1M40

ULTRA HIGH RESOLUTION CRYSTAL STRUCTURE OF TEM-1

Replaces:  1L7U
Summary for 1M40
Entry DOI10.2210/pdb1m40/pdb
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 formula weight29683.33
Authors
Minasov, G.,Wang, X.,Shoichet, B.K. (deposition date: 2002-07-01, release date: 2002-07-17, Last modification date: 2021-10-27)
Primary citationMinasov, 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
Cited by
PubMed: 11996574
DOI: 10.1021/ja0259640
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (0.85 Å)
Structure validation

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