Structure of PDB 4mvc Chain B Binding Site BS01

Receptor Information
>4mvc Chain B (length=204) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFH
SGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHC
RYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAG
MFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRQKWEEKSREFIGSFLE
MFGP
Ligand information
Ligand IDCDC
InChIInChI=1S/C14H26N4O11P2/c1-18(2,3)6-7-26-30(22,23)29-31(24,25)27-8-9-11(19)12(20)13(28-9)17-5-4-10(15)16-14(17)21/h4-5,9,11-13,19-20H,6-8H2,1-3H3,(H3-,15,16,21,22,23,24,25)/t9-,11-,12-,13-/m1/s1
InChIKeyRZZPDXZPRHQOCG-OJAKKHQRSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C[N+](C)(C)CCOP(=O)([O-])OP(=O)(O)OCC1C(C(C(O1)N2C=CC(=NC2=O)N)O)O
OpenEye OEToolkits 1.5.0C[N+](C)(C)CCO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)N2C=CC(=NC2=O)N)O)O
CACTVS 3.341C[N+](C)(C)CCO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N2C=CC(=NC2=O)N
CACTVS 3.341C[N+](C)(C)CCO[P]([O-])(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O)N2C=CC(=NC2=O)N
ACDLabs 10.04[O-]P(=O)(OCC[N+](C)(C)C)OP(=O)(O)OCC2OC(N1C(=O)N=C(N)C=C1)C(O)C2O
FormulaC14 H26 N4 O11 P2
Name[2-CYTIDYLATE-O'-PHOSPHONYLOXYL]-ETHYL-TRIMETHYL-AMMONIUM
ChEMBLCHEMBL1231700
DrugBankDB12153
ZINC
PDB chain4mvc Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4mvc Structural Basis for Autoinhibition of CTP:Phosphocholine Cytidylyltransferase (CCT), the Regulatory Enzyme in Phosphatidylcholine Synthesis, by Its Membrane-binding Amphipathic Helix.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		D82 G83 I84 F85 H92 A95 W151 H168 D169 Y173 Y182 R196 T197
Binding residue
(residue number reindexed from 1)		D43 G44 I45 F46 H53 A56 W112 H129 D130 Y134 Y143 R157 T158
Annotation score4
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.
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

View graph for
Molecular Function
View graph for
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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