Structure of PDB 3s22 Chain A

Receptor sequence
>3s22A (length=361) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
APADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGR
RVTPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSRFD
GISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYS
NPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQ
GYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQA
LDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARL
PAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVK
IAYAILSGLEQ
3D structure
PDB3s22 Side chain SAR of bicyclic Beta-lactamase inhibitors (BLIs). 2. N-Alkylated and open chain analogs of MK-8712
ChainA
Resolution1.65 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) S62 K65 Y149 E271 K314 S317
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 3S2 A S90 Q146 Y177 N179 Y249 T343 G344 S345 S62 Q118 Y149 N151 Y221 T315 G316 S317 PDBbind-CN: -logKd/Ki=5.46,IC50=3.5uM
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:3s22, PDBe:3s22, PDBj:3s22
PDBsum3s22
PubMed21676616
UniProtP24735|AMPC_PSEAE Beta-lactamase (Gene Name=ampC)

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