Structure of PDB 4pvo Chain A Binding Site BS04

Receptor Information
>4pvo Chain A (length=231) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELL
LIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGV
ATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYP
EAQFVIPGHGLPGGLDLLKHTTNVVKAHTNR
Ligand information
Ligand IDSVB
InChIInChI=1S/C17H17Cl3N4O2S2/c1-22-4-6-23(7-5-22)21-14(25)9-24-16(26)13(28-17(24)27)8-10-11(18)2-3-12(19)15(10)20/h2-3,8H,4-7,9H2,1H3,(H,21,25)/b13-8-
InChIKeyGTHJLNHVDYJCCB-JYRVWZFOSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CN1CCN(CC1)NC(=O)CN2C(=S)S\C(=C/c3c(Cl)ccc(Cl)c3Cl)C2=O
OpenEye OEToolkits 1.7.6CN1CCN(CC1)NC(=O)CN2C(=O)C(=Cc3c(ccc(c3Cl)Cl)Cl)SC2=S
ACDLabs 12.01O=C(NN1CCN(C)CC1)CN2C(=O)C(\SC2=S)=C\c3c(Cl)ccc(Cl)c3Cl
OpenEye OEToolkits 1.7.6CN1CCN(CC1)NC(=O)CN2C(=O)/C(=C/c3c(ccc(c3Cl)Cl)Cl)/SC2=S
CACTVS 3.385CN1CCN(CC1)NC(=O)CN2C(=S)SC(=Cc3c(Cl)ccc(Cl)c3Cl)C2=O
FormulaC17 H17 Cl3 N4 O2 S2
NameN-(4-methylpiperazin-1-yl)-2-[(5Z)-4-oxo-2-thioxo-5-(2,3,6-trichlorobenzylidene)-1,3-thiazolidin-3-yl]acetamide
ChEMBLCHEMBL4068716
DrugBank
ZINC
PDB chain4pvo Chain A Residue 404 [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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PDB4pvo Rhodanine hydrolysis leads to potent thioenolate mediated metallo-beta-lactamase inhibition.
Resolution1.48 Å
Binding residue
(original residue number in PDB)		F61 Y67 N233 H263
Binding residue
(residue number reindexed from 1)		F31 Y36 N179 H209
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=6.31,IC50=0.49uM
Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 D120 H196 C221 Y224 N233 H263
Catalytic site (residue number reindexed from 1) H83 H85 D87 H148 C167 Y170 N179 H209
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4pvo, PDBe:4pvo, PDBj:4pvo
PDBsum4pvo
PubMed25411887
UniProtQ9K2N0

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