5VMQ

STRUCTURE OF THE R105A MUTANT CATALYTIC TRIMER OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE AT 2.0-A RESOLUTION

Replaces:  1GQ3

Summary for 5VMQ

• Entry DOI: 10.2210/pdb5vmq/pdb
• Descriptor: Aspartate carbamoyltransferase, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: rossman fold, mutant, pyrimidine biosynthesis, aspartate carbamoyltransferase, transferase
• Biological source: Escherichia coli O45:K1 (strain S88 / ExPEC)
• Total number of polymer chains: 3
• Total formula weight: 102828.51

Authors

Beernink, P.T.,Endrizzi, J.A. (deposition date: 2017-04-28, release date: 2017-05-24, Last modification date: 2024-03-13)

• Primary citation: Endrizzi, J.A.,Beernink, P.T.; Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.; Protein Sci., 26:2221-2228, 2017; PubMed: 28833948; DOI: 10.1002/pro.3277

Experimental method

X-RAY DIFFRACTION (2.012 Å)