Structure of PDB 6rpn Chain A

Receptor sequence
>6rpnA (length=232) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
GEYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDEL
LLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAG
VATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHS
TDNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHY
PEAQFVIPGHGLPGGLDLLKHTTNVVKAHTNR
3D structure
PDB6rpn Broad Spectrum beta-Lactamase Inhibition by a Thioether Substituted Bicyclic Boronate.
ChainA
Resolution1.409 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) H84 H86 D88 H149 C168 Y171 N180 H210
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 KDZ A F62 Y67 W87 H114 H116 D118 H179 C198 G209 N210 H240 F32 Y37 W57 H84 H86 D88 H149 C168 G179 N180 H210 MOAD: ic50=0.2uM
BS02 KL8 A F62 Y67 W87 H116 D118 H179 C198 N210 H240 F32 Y37 W57 H86 D88 H149 C168 N180 H210 MOAD: ic50=0.2uM
BS03 ZN A H114 H116 H179 H84 H86 H149
BS04 ZN A D118 C198 H240 D88 C168 H210
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:6rpn, PDBe:6rpn, PDBj:6rpn
PDBsum6rpn
PubMed31841636
UniProtQ9K2N0

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