Structure of PDB 4k4c Chain D Binding Site BS03

Receptor Information
>4k4c Chain D (length=137) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPF
GLLHGGASAALAETLGSMAGFMMTRDGQCVVGTELNATHHRPVSEGKVRG
VCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVLG
Ligand information
Ligand ID0FQ
InChIInChI=1S/C29H42N7O17P3S/c1-29(2,24(40)27(41)32-9-8-20(38)31-10-11-57-13-18(37)17-6-4-3-5-7-17)14-50-56(47,48)53-55(45,46)49-12-19-23(52-54(42,43)44)22(39)28(51-19)36-16-35-21-25(30)33-15-34-26(21)36/h3-7,15-16,19,22-24,28,39-40H,8-14H2,1-2H3,(H,31,38)(H,32,41)(H,45,46)(H,47,48)(H2,30,33,34)(H2,42,43,44)/t19-,22-,23-,24+,28-/m1/s1
InChIKeyWOEFYXMDPBOUAP-VXAHOBLNSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.2CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCSCC(=O)c4ccccc4)O
CACTVS 3.370CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCSCC(=O)c4ccccc4
CACTVS 3.370CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[C@@H](O)C(=O)NCCC(=O)NCCSCC(=O)c4ccccc4
OpenEye OEToolkits 1.7.2CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCSCC(=O)c4ccccc4)O
ACDLabs 12.01O=C(c1ccccc1)CSCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC4OC(n3cnc2c(ncnc23)N)C(O)C4OP(=O)(O)O
FormulaC29 H42 N7 O17 P3 S
Namephenacyl coenzyme A
ChEMBL
DrugBank
ZINCZINC000214185742
PDB chain4k4c Chain D Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4k4c Structure and Catalysis in the Escherichia coli Hotdog-fold Thioesterase Paralogs YdiI and YbdB.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		Q48 P49 L53 H54 G55 H89 H90 R91 P92
Binding residue
(residue number reindexed from 1)		Q48 P49 L53 H54 G55 H89 H90 R91 P92
Annotation score3
Binding affinityMOAD: Ki=65uM
Enzymatic activity
Enzyme Commision number 3.1.2.-
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016289 acyl-CoA hydrolase activity
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0016790 thiolester hydrolase activity
GO:0042802 identical protein binding
GO:0061522 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
Biological Process
GO:0009239 enterobactin biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
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Cellular Component
External links
PDB RCSB:4k4c, PDBe:4k4c, PDBj:4k4c
PDBsum4k4c
PubMed25010423
UniProtP0A8Y8|ENTH_ECOLI Proofreading thioesterase EntH (Gene Name=entH)

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