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
SO4 Sulfate ion
C2G [cytidine-5'-phosphate] glycerylphosphoric acid ester
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1N1D   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol
Release Data : 2003-11-11
Compound :
mol_id molecule chains synonym
1 glycerol-3-phosphate cytidylyltransferase A,B,C,D GCT, CDP-glycerol pyrophosphorylase, Teichoic acid biosynthesis protein D
ec: 2.7.7.39
Source :
mol_id organism_scientific expression_system
1 Bacillus subtilis  (taxid:1423) Escherichia coli  (taxid:562)
expression_system_strain: BL21(DE3)pLysS
expression_system_vector_type: PLASMID
expression_system_plasmid: pET11a
Authors : Pattridge, K.A., Weber, C.H., Friesen, J.A., Sankar, S., Kent, C., Ludwig, M.L.
Keywords : alpha/beta fold, cytidylyltransferase, nucleotidyltransferase, negative cooperativity, CDP-glycerol, transferase
Exp. method : X-RAY DIFFRACTION ( 2 Å )
Citation :

Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis

Pattridge, K.A.,Weber, C.H.,Friesen, J.A.  et al.
(2003)  J.Biol.Chem.  278 : 51863 - 51871

PubMed: 14506262
DOI: 10.1074/jbc.M306174200

A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis

Weber, C.H.,Park, Y.S.,Sanker, S.  et al.
(1999)  Structure  7 : 1113 - 1124

DOI: 10.1016/S0969-2126(99)80178-6

Chain : A, B, C, D
UniProt : P27623 (TAGD_BACSU)
Reaction: EC: Evidence:
Physiological Direction:
CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol + diphosphate 2.7.7.39 PubMed:14506262, PubMed:8393871
-