Structure of PDB 6jn6 Chain A

Receptor sequence
>6jn6A (length=231) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
EYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELL
LIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGV
ATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYP
EAQFVIPGHGLPGGLDLLKHTTNVVKAHTNR
3D structure
PDB6jn6 Structure-Based Development of (1-(3'-Mercaptopropanamido)methyl)boronic Acid Derived Broad-Spectrum, Dual-Action Inhibitors of Metallo- and Serine-beta-lactamases.
ChainA
Resolution1.602 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 H114 H116 H179 H83 H85 H148
BS02 ZN A D118 C198 H240 D87 C167 H209
BS03 BY0 A F62 W87 H116 D118 H179 R205 N210 F31 W56 H85 D87 H148 R174 N179 MOAD: Ki=0.07uM
PDBbind-CN: -logKd/Ki=7.15,Ki=0.07uM
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:6jn6, PDBe:6jn6, PDBj:6jn6
PDBsum6jn6
PubMed31269398
UniProtQ9K2N0

[Back to BioLiP]