Structure of PDB 8fqm Chain A

Receptor sequence
>8fqmA (length=357) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
TPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDK
KAVNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPI
DQVNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYS
NPSIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAF
GYNQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRA
INETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAI
SKEPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAY
VVLNAIK
3D structure
PDB8fqm Synthesis of a Novel Boronic Acid Transition State Inhibitor, MB076: A Heterocyclic Triazole Effectively Inhibits Acinetobacter -Derived Cephalosporinase Variants with an Expanded-Substrate Spectrum.
ChainA
Resolution1.53 Å
3D
structure
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Enzymatic activity
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 GLY A Q120 Y222 Q119 Y221
BS02 YDB A S64 Y150 Y222 G314 S315 T316 S317 R340 N343 S63 Y149 Y221 G313 S314 T315 S316 R339 N342
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8fqm, PDBe:8fqm, PDBj:8fqm
PDBsum8fqm
PubMed37358467
UniProtQ6DRA1

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