Structure of PDB 4mvc Chain A

Receptor sequence
>4mvcA (length=205) Species: 10116 (Rattus norvegicus) [Search protein sequence]
GLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFH
SGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHC
RYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAG
MFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRIQKWEEKSREFIGSFL
EMFGP
3D structure
PDB4mvc Structural Basis for Autoinhibition of CTP:Phosphocholine Cytidylyltransferase (CCT), the Regulatory Enzyme in Phosphatidylcholine Synthesis, by Its Membrane-binding Amphipathic Helix.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F121 G123
Catalytic site (residue number reindexed from 1) F82 G84
Enzyme Commision number 2.7.7.15: choline-phosphate cytidylyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CDC A D82 G83 I84 F85 G91 A95 K122 W151 H168 D169 Y173 Y182 R196 T197 I200 D43 G44 I45 F46 G52 A56 K83 W112 H129 D130 Y134 Y143 R157 T158 I161
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004105 choline-phosphate cytidylyltransferase activity
Biological Process
GO:0006657 CDP-choline pathway
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4mvc, PDBe:4mvc, PDBj:4mvc
PDBsum4mvc
PubMed24275660
UniProtP19836|PCY1A_RAT Choline-phosphate cytidylyltransferase A (Gene Name=Pcyt1a)

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