Structure of PDB 5waf Chain D

Receptor sequence
>5wafD (length=355) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
PKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKK
AVNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPID
QVNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYSN
PSIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFG
YNQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRAI
NETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAIS
KEPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAYV
VLNAI
3D structure
PDB5waf Structure-Based Analysis of Boronic Acids as Inhibitors of Acinetobacter-Derived Cephalosporinase-7, a Unique Class C beta-Lactamase.
ChainD
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) S62 K65 Y148 E270 K310 S313
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 D S64 L119 Q120 Y150 V212 N213 T313 G314 S315 T316 S317 R340 S62 L117 Q118 Y148 V210 N211 T311 G312 S313 T314 S315 R338
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:5waf, PDBe:5waf, PDBj:5waf
PDBsum5waf
PubMed29144724
UniProtQ6DRA1

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