1G23

THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). GLUCOSE-1-PHOSPHATE COMPLEX.

Summary for 1G23

Entry DOI	10.2210/pdb1g23/pdb
Related	1fxo 1fzw 1g0r 1g1l 1g2v 1g31
Descriptor	GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE, 1-O-phosphono-alpha-D-glucopyranose, SULFATE ION (3 entities in total)
Functional Keywords	l-rhamnose, nucleotidyltransferase, pyrophosphorylase, thymidylyltransferase, allostery, transferase
Biological source	Pseudomonas aeruginosa
Total number of polymer chains	8
Total formula weight	264741.28
Authors	Blankenfeldt, W.,Asuncion, M.,Lam, J.S.,Naismith, J.H. (deposition date: 2000-10-16, release date: 2000-12-27, Last modification date: 2020-07-29)
Primary citation	Blankenfeldt, W.,Asuncion, M.,Lam, J.S.,Naismith, J.H. The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA). EMBO J., 19:6652-6663, 2000 Cited by PubMed: 11118200 DOI: 10.1093/emboj/19.24.6652 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation