Structure of PDB 5lsc Chain A

Receptor sequence
>5lscA (length=235) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
SGEYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDE
LLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAA
GVATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAH
STDNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQH
YPEAQFVIPGHGLPGGLDLLKHTTNVVKAHTNRSV
3D structure
PDB5lsc The structure of the metallo-beta-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor.
ChainA
Resolution1.497 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) H116 H118 D120 H196 C221 Y224 N233 H263
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 752 A Y67 W87 H118 D119 D120 H196 C221 N233 H263 Y38 W58 H87 D88 D89 H150 C169 N181 H211 MOAD: ic50=20uM
PDBbind-CN: -logKd/Ki=4.70,IC50=20uM
BS02 ZN A H116 H118 H196 H85 H87 H150
BS03 ZN A D120 C221 H263 D89 C169 H211
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:5lsc, PDBe:5lsc, PDBj:5lsc
PDBsum5lsc
PubMed27834790
UniProtB8QIQ9

[Back to BioLiP]