Structure of PDB 5n4s Chain A Binding Site BS03

Receptor Information
>5n4s 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]
AYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELL
LIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGV
ATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYP
EAQFVIPGHGLPGGLDLLKHTTNVVKAHTNR
Ligand information
Ligand IDR38
InChIInChI=1S/C15H18N2O3S/c1-9(8-21)14(18)17-13(15(19)20)6-10-7-16-12-5-3-2-4-11(10)12/h2-5,7,9,13,16,21H,6,8H2,1H3,(H,17,18)(H,19,20)/t9-,13-/m1/s1
InChIKeyZOUTYVWHWSUKPL-NOZJJQNGSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6CC(CS)C(=O)NC(Cc1c[nH]c2c1cccc2)C(=O)O
CACTVS 3.385C[C@H](CS)C(=O)N[C@H](Cc1c[nH]c2ccccc12)C(O)=O
OpenEye OEToolkits 2.0.6C[C@H](CS)C(=O)N[C@H](Cc1c[nH]c2c1cccc2)C(=O)O
CACTVS 3.385C[CH](CS)C(=O)N[CH](Cc1c[nH]c2ccccc12)C(O)=O
FormulaC15 H18 N2 O3 S
Name(2~{R})-3-(1~{H}-indol-3-yl)-2-[[(2~{S})-2-methyl-3-sulfanyl-propanoyl]amino]propanoic acid
ChEMBLCHEMBL4177035
DrugBank
ZINC
PDB chain5n4s Chain A 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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PDB5n4s Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-beta-lactamase inhibition.
Resolution1.2 Å
Binding residue
(original residue number in PDB)		Y67 H116 D118 H179 R205 G209 N210 H240
Binding residue
(residue number reindexed from 1)		Y36 H85 D87 H148 R174 G178 N179 H209
Annotation score1
Binding affinityMOAD: ic50=0.055uM
PDBbind-CN: -logKd/Ki=7.26,IC50=0.055uM
Enzymatic activity
Catalytic site (original residue number in PDB) H114 H116 D118 H179 C198 Y201 N210 H240
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5n4s, PDBe:5n4s, PDBj:5n4s
PDBsum5n4s
PubMed28470248
UniProtQ9K2N0

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