Structure of PDB 1u7z Chain B Binding Site BS01

Receptor Information
>1u7z Chain B (length=218) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SPVNDLKHLNIMITAGPTREPLDPVRYISDHSSGKMGFAIAAAAARRGAN
VTLVSGPVSLPTPPFVKRVDVMTALEMEAAVNASVQQQNIFIGCAAVADY
RAATVAPEKIELTIKMVKNPDIVAGVAALKDHRPYVVGFAAETNNVEEYA
RQKRIRKNLDLICANDVSQPTQGFNSDNNALHLFWQDGDKVLPLERKELL
GQLLLDEIVTRYDEKNRR
Ligand information
Ligand IDPMT
InChIInChI=1S/C18H30N4O15P2/c1-18(2,8-35-38(29,30)31)14(26)15(27)20-5-3-11(23)37-39(32,33)34-7-9-12(24)13(25)16(36-9)22-6-4-10(19)21-17(22)28/h4,6,9,12-14,16,24-26H,3,5,7-8H2,1-2H3,(H,20,27)(H,32,33)(H2,19,21,28)(H2,29,30,31)/t9-,12-,13-,14+,16-/m1/s1
InChIKeyJURRMAHLXBVXRF-FIEZRUJPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(C)(CO[P](O)(O)=O)[CH](O)C(=O)NCCC(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O)N2C=CC(=NC2=O)N
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)N2C=CC(=NC2=O)N)O)O)O
CACTVS 3.341CC(C)(CO[P](O)(O)=O)[C@@H](O)C(=O)NCCC(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N2C=CC(=NC2=O)N
ACDLabs 10.04O=P(O)(O)OCC(C)(C)C(O)C(=O)NCCC(=O)OP(=O)(O)OCC2OC(N1C(=O)N=C(N)C=C1)C(O)C2O
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)O)C(C(=O)NCCC(=O)OP(=O)(O)OCC1C(C(C(O1)N2C=CC(=NC2=O)N)O)O)O
FormulaC18 H30 N4 O15 P2
NamePHOSPHORIC ACID MONO-[3-(3-{[5-(4-AMINO-2-OXO-2H-PYRIMIDIN-1-YL)-3,4- DIHYDROXY-TETRAHYDRO-FURAN-2- YLMETHOXY]-HYDROXY-PHOSPHORYLOXY}-3-OXO-PROPYLCARBAMOYL)-3-HYDROXY-2,2- DIMETHYL-PROPYL] ESTER;
4'-PHOSPHOPANTOTHENOYL- CYTIDINE-5'-MONOPHOSPHATE
ChEMBL
DrugBank
ZINCZINC000016051552
PDB chain1u7z Chain B Residue 1500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1u7z Structural Basis of CTP-Dependent Peptide Bond Formation in Coenzyme A Biosynthesis Catalyzed by Escherichia coli PPC Synthetase
Resolution2.3 Å
Binding residue
(original residue number in PDB)		S212 S213 G214 K215 M216 G273 C274 A275 A276 V277 P308 D309 I310 V311 F327 A329 K341 K345 N353 F362 K385
Binding residue
(residue number reindexed from 1)		S32 S33 G34 K35 M36 G93 C94 A95 A96 V97 P120 D121 I122 V123 F139 A141 K153 K157 N165 F174 K197
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) D210
Catalytic site (residue number reindexed from 1) D30
Enzyme Commision number 4.1.1.36: phosphopantothenoylcysteine decarboxylase.
6.3.2.5: phosphopantothenate--cysteine ligase (CTP).
Gene Ontology
Molecular Function
GO:0004632 phosphopantothenate--cysteine ligase activity
GO:0004633 phosphopantothenoylcysteine decarboxylase activity
GO:0010181 FMN binding
Biological Process
GO:0015937 coenzyme A biosynthetic process
GO:0015941 pantothenate catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1u7z, PDBe:1u7z, PDBj:1u7z
PDBsum1u7z
PubMed15530362
UniProtP0ABQ0|COABC_ECOLI Coenzyme A biosynthesis bifunctional protein CoaBC (Gene Name=coaBC)

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