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EBI PDBe PDBeView

PDBe Entry: 1fzw view

THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). APO ENZYME.
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.9 Å, R-factor: 18.0%, Free R-factor: 25.1%, Spacegroup: P 1
Released 27/12/2000, deposition: 04/10/2000, last revision: 24/02/2009
Authors Blankenfeldt, W.search; Asuncion, M.search; Lam, J.S.search; Naismith, J.H.search
Primary citation The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).
EMBO J.search vol:19, pag:6652-6663 (2000) [PubMed ID 11118200 ]search
Keywords rhamnosesearch, nucleotidyltransferasesearch, pyrophosphorylasesearch, thymidylyltransferasesearch, allosterysearch
EC 2.7.7.24 ExPASy BRENDA search (A B C D E F G H)
Organism Pseudomonas aeruginosa 287search(A B C D E F G H)
UniProt Glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24),Glucose-1-phosphate thymidylyltransferase (Glucose-1-phosphate thymidyltransferase) Q9HU22search (A B C D E F G H)
Solvent A, B, C, D, E, F, G, H
Related entries 1fxo, 1g0r, 1g1l, 1g23, 1g2v, 1g31
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D, E, F, G, H GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE Protein Q9HU22 (Q9HU22_PSEAE)search
 293 100%
Heterogens
Id Name Ligands
C, D, A, B, H, G, F, E SULFATE ION SO4 search
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