5VMQ
STRUCTURE OF THE R105A MUTANT CATALYTIC TRIMER OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE AT 2.0-A RESOLUTION
Replaces: 1GQ3Summary 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 Cited by PubMed: 28833948DOI: 10.1002/pro.3277 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.012 Å) |
Structure validation
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