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Ligands
Code Name Style Show Link
CDC [2-cytidylate-O'-phosphonyloxyl]-ethyl-trimethyl-ammonium
FMT Formic acid
GOL Glycerol
Non-standard Residues
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Glycosylation
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Code : 3HL4   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of a mammalian CTP:phosphocholine cytidylyltransferase with CDP-choline
Release Data : 2009-09-22
Compound :
mol_id molecule chains synonym
1 Choline-phosphate cytidylyltransferase A A,B Phosphorylcholine transferase A, CTP:phosphocholine cytidylyltransferase A, CCT A, CT A, CCT-alpha
ec: 2.7.7.15
fragment: Domain N and C
mutation: None
Source :
mol_id organism_scientific organism_common expression_system
1 Rattus norvegicus  (taxid:10116) Rat TRICHOPLUSIA NI  (taxid:7111)
gene: Ctpct, Pcyt1, Pcyt1a
expression_system_vector_type: BACULOVIRUS
expression_system_plasmid: PVL1393
Authors : Lee, J., Paetzel, M., Cornell, R.B.
Keywords : Cytidylyltransferase, Rossmann Fold, Phospholipid synthesis, Phosphatidylcholine, Phosphocholine, CTP, CDP-choline, Amphitropic protein, Lipid metabolism, Nucleotidyltransferase, Phosphoprotein, Transferase
Exp. method : X-RAY DIFFRACTION ( 2.20 Å )
Citation :

Crystal Structure of a mammalian CTP: Phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyl-transferase fold

Lee, J.,Johnson, J.E.,Ding, Z.  et al.
(2009)  J.Biol.Chem.  284 : 33535 - 33548

PubMed: 19783652
DOI: 10.1074/jbc.M109.053363

Chain : A, B
UniProt : P19836 (PCY1A_RAT)
Reaction: EC: Evidence:
Physiological Direction:
CTP + H(+) + phosphocholine = CDP-choline + diphosphate 2.7.7.15 PubMed:12718547, PubMed:19783652, PubMed:2166941, PubMed:639816, PubMed:8185307, PubMed:8381041
left-to-right PubMed:19783652