Structure of PDB 6ur3 Chain A

Receptor sequence
>6ur3A (length=363) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
GEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKED
GRRVTPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSR
FDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRL
YSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQY
AQGYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWA
QALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIA
RLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAER
VKIAYAILSGLEQ
3D structure
PDB6ur3 Serendipitous discovery of aryl boronic acids as beta-lactamase inhibitors.
ChainA
Resolution1.423 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S90 K93 Y177 E299 K342 S345
Catalytic site (residue number reindexed from 1) S64 K67 Y151 E273 K316 S319
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 QFP A S90 Y177 N179 Y249 T343 G344 S345 S64 Y151 N153 Y223 T317 G318 S319
BS02 EDO A R175 Y177 E299 M318 K342 R149 Y151 E273 M292 K316
BS03 EDO A E269 A276 D280 E243 A250 D254
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6ur3, PDBe:6ur3, PDBj:6ur3
PDBsum6ur3
PubMed31759850
UniProtP24735|AMPC_PSEAE Beta-lactamase (Gene Name=ampC)

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