Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
CB3 10-propargyl-5,8-dideazafolic acid
UMP 2'-deoxyuridine 5'-monophosphate
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1CI7   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII
Release Data : 2000-04-10
Compound :
mol_id molecule chains
1 PROTEIN (THYMIDYLATE SYNTHASE) A,B
ec: 2.1.1.45
other_details: COVALENT BOND BETWEEN C173 AND DUMP IN MONOMER A
Source :
mol_id organism_scientific expression_system
1 Pneumocystis carinii  (taxid:4754) Escherichia coli  (taxid:562)
cellular_location: CYTOPLASM
expression_system_strain: CHI2913
expression_system_cellular_location: CYTOPLASM
expression_system_vector_type: PLASMID
expression_system_plasmid: PUETS-1.8
Authors : Anderson, A.C., O'Neil, R.H., Delano, W.L., Stroud, R.M.
Keywords : METHYLTRANSFERASE, NUCLEOTIDE BIOSYNTHESIS, HALF-SITES REACTIVITY, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.6 Å )
Citation :

The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits.

Anderson, A.C.,O'Neil, R.H.,DeLano, W.L.  et al.
(1999)  Biochemistry  38 : 13829 - 13836

PubMed: 10529228
DOI: 10.1021/bi991610i

Chain : A, B
UniProt : P13100 (TYSY_PNECA)
Reaction: EC: Evidence:
Physiological Direction:
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8- dihydrofolate + dTMP 2.1.1.45 -
-