Structure of PDB 5waf Chain B

Receptor sequence
>5wafB (length=358) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
TPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDK
KAVNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPI
DQVNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYS
NPSIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAF
GYNQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRA
INETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAI
SKEPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAY
VVLNAIKK
3D structure
PDB5waf Structure-Based Analysis of Boronic Acids as Inhibitors of Acinetobacter-Derived Cephalosporinase-7, a Unique Class C beta-Lactamase.
ChainB
Resolution2.03 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) S63 K66 Y149 E271 K311 S314
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 A0Y B S64 Q120 Y150 V212 N213 T313 G314 S315 T316 S317 R340 S63 Q119 Y149 V211 N212 T312 G313 S314 T315 S316 R339
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:5waf, PDBe:5waf, PDBj:5waf
PDBsum5waf
PubMed29144724
UniProtQ6DRA1

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