Structure of PDB 4pvt Chain A

Receptor sequence
>4pvtA (length=231) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
EYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELL
LIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGV
ATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYP
EAQFVIPGHGLPGGLDLLKHTTNVVKAHTNR
3D structure
PDB4pvt Rhodanine hydrolysis leads to potent thioenolate mediated metallo-beta-lactamase inhibition.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 D120 H196 C221 Y224 N233 H263
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 H116 H118 H196 H83 H85 H148
BS02 ZN A D120 C221 H263 D87 C167 H209
BS03 S3C A W87 H118 D120 H196 C221 N233 H263 W56 H85 D87 H148 C167 N179 H209 PDBbind-CN: -logKd/Ki=6.52,IC50=0.3uM
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4pvt, PDBe:4pvt, PDBj:4pvt
PDBsum4pvt
PubMed25411887
UniProtQ9K2N0

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