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Ligands
Code Name Style Show Link
TMF 5,10-methylene-6-hydrofolic acid
UFP 5-fluoro-2'-deoxyuridine-5'-monophosphate
Non-standard Residues
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CXM N-carboxymethionine
Glycosylation
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Code : 1BJG   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : D221(169)N MUTANT DOES NOT PROMOTE OPENING OF THE COFACTOR IMIDAZOLIDINE RING
Release Data : 1998-11-04
Compound :
mol_id molecule chains
1 THYMIDYLATE SYNTHASE A
ec: 2.1.1.45
mutation: D169N
Source :
mol_id organism_scientific
1 Escherichia coli  (taxid:562)
cell_line: X2913
plasmid: PTHYA-D169N
Authors : Sage, C.R., Michelitsch, M.D., Finer-Moore, J., Stroud, R.M.
Keywords : TRANSFERASE, ACTIVE SITE MUTANT, REACTION INTERMEDIATE METHYLTRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.3 Å )
Citation :

D221 in thymidylate synthase controls conformation change, and thereby opening of the imidazolidine.

Sage, C.R.,Michelitsch, M.D.,Stout, T.J.  et al.
(1998)  Biochemistry  37 : 13893 - 13901

PubMed: 9753479
DOI: 10.1021/bi9810510

Stereochemistry of a Multistep/Bipartite Methyl Transfer Reaction: Thymidylate Synthase

Stroud, R.M.,Finer-Moore, J.S.
(1993)  Faseb J.  7 : 671

Structure, Multiple Site Binding, and Segmental Accommodation in Thymidylate Synthase on Binding Dump and an Anti-Folate

Montfort, W.R.,Perry, K.M.,Fauman, E.B.  et al.
(1990)  Biochemistry  29 : 6964

Erratum. Structure, Multiple Site Binding, and Segmental Accommodation in Thymidylate Synthase on Binding Dump and an Anti-Folate

Montfort, W.R.,Perry, K.M.,Fauman, E.B.  et al.
(1990)  Biochemistry  29 : 10864

Chain : A
UniProt : P0A884 (TYSY_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8- dihydrofolate + dTMP 2.1.1.45 HAMAP-Rule:MF_00008, PubMed:2223754, PubMed:3286637, PubMed:9826509
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