Structure of PDB 4x68 Chain B

Receptor sequence
>4x68B (length=357) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
MDRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRV
TPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSRFDGI
SLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYSNP
SIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGY
GKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALD
ATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARLPA
PQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIA
YAILSGL
3D structure
PDB4x68 OP0595, a new diazabicyclooctane: mode of action as a serine beta-lactamase inhibitor, antibiotic and beta-lactam 'enhancer'
ChainB
Resolution1.68 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) S60 K63 Y147 E269 K312 S315
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 OP0 B S90 Q146 Y177 Y249 T343 G344 S345 S60 Q116 Y147 Y219 T313 G314 S315 PDBbind-CN: -logKd/Ki=6.57,IC50=271nM
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:4x68, PDBe:4x68, PDBj:4x68
PDBsum4x68
PubMed26089439
UniProtP24735|AMPC_PSEAE Beta-lactamase (Gene Name=ampC)

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