Structure of PDB 3hl4 Chain B Binding Site BS01

Receptor Information
>3hl4 Chain B (length=177) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFH
SGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHC
RYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAG
MFAPTQRTEGISTSDIITRIVRDYDVY
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 chain3hl4 Chain B Residue 237 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3hl4 Crystal Structure of a mammalian CTP: Phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyl-transferase fold
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D82 G83 I84 F85 G91 H92 A95 C113 K122 W151 H168 D169 Y173 Y182 R196 T197
Binding residue
(residue number reindexed from 1)		D43 G44 I45 F46 G52 H53 A56 C74 K83 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

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Molecular Function
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Biological Process
External links
PDB RCSB:3hl4, PDBe:3hl4, PDBj:3hl4
PDBsum3hl4
PubMed19783652
UniProtP19836|PCY1A_RAT Choline-phosphate cytidylyltransferase A (Gene Name=Pcyt1a)

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