Structure of PDB 5wae Chain A

Receptor sequence
>5waeA (length=355) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
KDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKA
VNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPIDQ
VNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYSNP
SIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGY
NQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRAIN
ETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAISK
EPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAYVV
LNAIK
3D structure
PDB5wae Structure-Based Analysis of Boronic Acids as Inhibitors of Acinetobacter-Derived Cephalosporinase-7, a Unique Class C beta-Lactamase.
ChainA
Resolution1.804 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) S61 K64 Y147 E269 K309 S312
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 A1J A S64 Y150 V212 Y222 T313 G314 S315 S317 S61 Y147 V209 Y219 T310 G311 S312 S314 PDBbind-CN: -logKd/Ki=6.80,Ki=160nM
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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Cellular Component
External links
PDB RCSB:5wae, PDBe:5wae, PDBj:5wae
PDBsum5wae
PubMed29144724
UniProtQ6DRA1

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