Structure of PDB 5w14 Chain A

Receptor sequence
>5w14A (length=356) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
KDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKA
VNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPIDQ
VNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYSNP
SIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGY
NQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRAIN
ETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAISK
EPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAYVV
LNAIKK
3D structure
PDB5w14 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) 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 9TJ A S64 Y150 Y222 G314 S315 S317 R340 S61 Y147 Y219 G311 S312 S314 R337 PDBbind-CN: -logKd/Ki=7.34,Ki=46nM
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:5w14, PDBe:5w14, PDBj:5w14
PDBsum5w14
PubMed29144725
UniProtQ6DRA1

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