1G3L

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

Summary for 1G3L

Entry DOI	10.2210/pdb1g3l/pdb
Related	1fxo 1fzw 1g0r 1g1l 1g23 1g2v
Descriptor	GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE, SULFATE ION, 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE (3 entities in total)
Functional Keywords	l-rhamnose, nucleotidyltransferase, pyrophosphorylase, thymidylyltransferase, allostery, transferase
Biological source	Pseudomonas aeruginosa
Total number of polymer chains	4
Total formula weight	134822.33
Authors	Blankenfeldt, W.,Asuncion, M.,Lam, J.S.,Naismith, J.H. (deposition date: 2000-10-24, release date: 2000-12-27, Last modification date: 2023-08-09)
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 (2.7 Å)

Structure validation