Structure of PDB 4hef Chain A

Receptor sequence
>4hefA (length=360) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
APADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGR
RVTPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSRFD
GISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYS
NPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQ
GYGKRDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQA
LDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARL
PAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVK
IAYAILSGLE
3D structure
PDB4hef Structural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC beta-Lactamases
ChainA
Resolution1.86 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 G142 P144 P148 Y177 G183 E299 K342 S345
Catalytic site (residue number reindexed from 1) S62 K65 G114 P116 P120 Y149 G155 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 NXL A S90 Q146 Y177 T343 G344 S345 S62 Q118 Y149 T315 G316 S317
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:4hef, PDBe:4hef, PDBj:4hef
PDBsum4hef
PubMed23439634
UniProtP24735|AMPC_PSEAE Beta-lactamase (Gene Name=ampC)

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