Structure of PDB 5n4s Chain B Binding Site BS02

Receptor Information
>5n4s Chain B (length=230) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AYPTVEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLL
IDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVA
TYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHSTD
NLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYPE
AQFVIPGHGLPGGLDLLKHTTNVVKAHTNR
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5n4s Chain B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
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)		H114 H116 H179
Binding residue
(residue number reindexed from 1)		H82 H84 H147
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H114 H116 D118 H179 C198 Y201 N210 H240
Catalytic site (residue number reindexed from 1) H82 H84 D86 H147 C166 Y169 N178 H208
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

[Back to BioLiP]