BioLiP

Structure of PDB 5n4t Chain A

Receptor sequence

>5n4tA (length=234) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]

SGEYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDE
LLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAA
GVATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAH
STDNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQH
YPEAQFVIPGHGLPGGLDLLKHTTNVVKAHTNRS

3D structure

PDB

5n4t Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-beta-lactamase inhibition.

Chain

Resolution

1.16 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H114 H116 D118 H179 C198 Y201 N210 H240
Catalytic site (residue number reindexed from 1)	H85 H87 D89 H150 C169 Y172 N181 H211
Enzyme Commision number	3.5.2.6: beta-lactamase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	H114 H116 H179	H85 H87 H150
BS02	ZN	A	D118 C198 H240	D89 C169 H211
BS03	R59	A	Y67 W87 D118 H179 R205 N210 H240	Y38 W58 D89 H150 R176 N181 H211	MOAD: ic50=1.06uM PDBbind-CN: -logKd/Ki=5.97,IC50=1.06uM

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

PDB	RCSB:5n4t, PDBe:5n4t, PDBj:5n4t
PDBsum	5n4t
PubMed	28470248
UniProt	Q9K2N0