Structure of PDB 5w13 Chain A

Receptor sequence
>5w13A (length=354) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
DQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKAV
NSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPIDQV
NLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYSNPS
IGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGYN
QENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRAINE
THQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAISKE
PSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAYVVL
NAIK
3D structure
PDB5w13 Inhibition of Acinetobacter-Derived Cephalosporinase: Exploring the Carboxylate Recognition Site Using Novel beta-Lactamase Inhibitors.
ChainA
Resolution1.95 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) S60 K63 Y146 E268 K308 S311
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 SM2 A S64 L119 Y150 G314 S315 T316 R340 S60 L115 Y146 G310 S311 T312 R336 PDBbind-CN: -logKd/Ki=7.66,Ki=22nM
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:5w13, PDBe:5w13, PDBj:5w13
PDBsum5w13
PubMed29144725
UniProtQ6DRA1

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