Structure of PDB 6nb1 Chain A Binding Site BS01

Receptor Information
>6nb1 Chain A (length=188) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ALVPMVIEERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENP
EKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTA
GAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMAL
HTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN
Ligand information
Ligand IDKHS
InChIInChI=1S/C18H18ClF3N2O3S2/c1-17(2,16(25)23-9-10-28-14-6-4-3-5-13(14)19)29(26,27)15-8-7-12(11-24-15)18(20,21)22/h3-8,11H,9-10H2,1-2H3,(H,23,25)
InChIKeyOUZIIFOEMPAZKX-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(C)(C(=O)NCCSc1ccccc1Cl)[S](=O)(=O)c2ccc(cn2)C(F)(F)F
OpenEye OEToolkits 2.0.6CC(C)(C(=O)NCCSc1ccccc1Cl)S(=O)(=O)c2ccc(cn2)C(F)(F)F
ACDLabs 12.01Clc1ccccc1SCCNC(=O)C(C)(C)S(=O)(=O)c2ccc(cn2)C(F)(F)F
FormulaC18 H18 Cl F3 N2 O3 S2
NameN-{2-[(2-chlorophenyl)sulfanyl]ethyl}-2-methyl-2-{[5-(trifluoromethyl)pyridin-2-yl]sulfonyl}propanamide
ChEMBLCHEMBL4594004
DrugBank
ZINC
PDB chain6nb1 Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6nb1 ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		R36 L37 E40 V42 Y74 Y76 F126 R206
Binding residue
(residue number reindexed from 1)		R17 L18 E21 V23 Y55 Y57 F107 R187
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G82 S111 M112 H136 D185
Catalytic site (residue number reindexed from 1) G63 S92 M93 H117 D166
Enzyme Commision number 3.4.21.92: endopeptidase Clp.
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0042802 identical protein binding
GO:0051117 ATPase binding
Biological Process
GO:0006508 proteolysis
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
GO:0009266 response to temperature stimulus
GO:0009314 response to radiation
GO:0009408 response to heat
GO:0010498 proteasomal protein catabolic process
GO:0043068 positive regulation of programmed cell death
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009368 endopeptidase Clp complex
GO:0009376 HslUV protease complex
GO:0016020 membrane

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6nb1, PDBe:6nb1, PDBj:6nb1
PDBsum6nb1
PubMed31925204
UniProtP0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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