Structure of PDB 5w12 Chain A

Receptor sequence
>5w12A (length=353) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
QEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKAVN
SNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPIDQVN
LLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYSNPSI
GLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGYNQ
ENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRAINET
HQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAISKEP
SVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAYVVLN
AIK
3D structure
PDB5w12 Inhibition of Acinetobacter-Derived Cephalosporinase: Exploring the Carboxylate Recognition Site Using Novel beta-Lactamase Inhibitors.
ChainA
Resolution1.88 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) S59 K62 Y145 E267 K307 S310
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 9TG A S64 Y150 S315 T316 R340 N343 S59 Y145 S310 T311 R335 N338 PDBbind-CN: -logKd/Ki=7.28,Ki=53nM
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:5w12, PDBe:5w12, PDBj:5w12
PDBsum5w12
PubMed29144725
UniProtQ6DRA1

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