Structure of PDB 2fzs Chain D Binding Site BS01

Receptor Information
>2fzs Chain D (length=185) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LVPMVIESFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKD
IYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAK
GKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTG
QSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN
Ligand information
Ligand IDCMQ
InChIInChI=1S/C24H32N2O5/c1-16(2)13-22(26-24(30)31-15-19-7-5-4-6-8-19)23(29)25-21(17(3)27)14-18-9-11-20(28)12-10-18/h4-12,16-17,21-22,27-28H,13-15H2,1-3H3,(H,25,29)(H,26,30)/t17-,21-,22-/m0/s1
InChIKeyZUWYQZGBCBSHFK-HSQYWUDLSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(OCc1ccccc1)NC(C(=O)NC(Cc2ccc(O)cc2)C(O)C)CC(C)C
OpenEye OEToolkits 1.5.0CC(C)C[C@@H](C(=O)N[C@@H](Cc1ccc(cc1)O)[C@H](C)O)NC(=O)OCc2ccccc2
CACTVS 3.341CC(C)C[CH](NC(=O)OCc1ccccc1)C(=O)N[CH](Cc2ccc(O)cc2)[CH](C)O
OpenEye OEToolkits 1.5.0CC(C)CC(C(=O)NC(Cc1ccc(cc1)O)C(C)O)NC(=O)OCc2ccccc2
CACTVS 3.341CC(C)C[C@H](NC(=O)OCc1ccccc1)C(=O)N[C@@H](Cc2ccc(O)cc2)[C@H](C)O
FormulaC24 H32 N2 O5
NameN~2~-[(BENZYLOXY)CARBONYL]-N-[(1S,2S)-2-HYDROXY-1-(4-HYDROXYBENZYL)PROPYL]-L-LEUCINAMIDE
ChEMBL
DrugBankDB07571
ZINCZINC000024799667
PDB chain2fzs Chain D Residue 504 [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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PDB2fzs Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G67 G68 V69 I70 S97 M98 H122 P124 L125 I142 M149
Binding residue
(residue number reindexed from 1)		G59 G60 V61 I62 S89 M90 H114 P116 L117 I134 M141
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G68 S97 M98 H122 D171
Catalytic site (residue number reindexed from 1) G60 S89 M90 H114 D163
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2fzs, PDBe:2fzs, PDBj:2fzs
PDBsum2fzs
PubMed16682229
UniProtP0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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