Structure of PDB 5wac Chain B

Receptor sequence
>5wacB (length=359) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
NTPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQD
KKAVNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTP
IDQVNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQY
SNPSIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYA
FGYNQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQR
AINETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTA
ISKEPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAA
YVVLNAIKK
3D structure
PDB5wac Structure-Based Analysis of Boronic Acids as Inhibitors of Acinetobacter-Derived Cephalosporinase-7, a Unique Class C beta-Lactamase.
ChainB
Resolution2.061 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y150 E272 K312 S315
Catalytic site (residue number reindexed from 1) S64 K67 Y150 E272 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 A1M B S64 Q120 Y150 V212 N213 T313 G314 S315 S317 S64 Q120 Y150 V212 N213 T313 G314 S315 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

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Biological Process
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Cellular Component
External links
PDB RCSB:5wac, PDBe:5wac, PDBj:5wac
PDBsum5wac
PubMed29144724
UniProtQ6DRA1

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