Structure of PDB 5n4s Chain A

Receptor sequence
>5n4sA (length=231) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
AYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELL
LIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGV
ATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYP
EAQFVIPGHGLPGGLDLLKHTTNVVKAHTNR
3D structure
PDB5n4s Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-beta-lactamase inhibition.
ChainA
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 D118 C198 H240 D87 C167 H209
BS02 ZN A H114 H116 H179 H83 H85 H148
BS03 R38 A Y67 H116 D118 H179 R205 G209 N210 H240 Y36 H85 D87 H148 R174 G178 N179 H209 MOAD: ic50=0.055uM
PDBbind-CN: -logKd/Ki=7.26,IC50=0.055uM
BS04 R38 A G64 A65 G33 A34 MOAD: ic50=0.055uM
PDBbind-CN: -logKd/Ki=7.26,IC50=0.055uM
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]