Structure of PDB 5wae Chain C Binding Site BS01

Receptor Information
>5wae Chain C (length=356) Species: 470 (Acinetobacter baumannii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKK
AVNSNTIFELGSVSKLFTATAGGYAKNKGKISFDDTPGKYWKELKNTPID
QVNLLQLATYTSGNLALQFPDEVQTDQQVLTFFKDWKPKNPIGEYRQYSN
PSIGLFGKVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFG
YNQENQPIRVNPGPLDAPAYGVKSTLPDMLSFIHANLNPQKYPTDIQRAI
NETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAIS
KEPSVKMYHKTGSTSGFGTYVVFIPKENIGLVMLTNKRIPNEERIKAAYV
VLNAIK
Ligand information
Ligand IDA1J
InChIInChI=1S/C9H13BNO9PS/c12-9(13)8-3-1-2-7(4-8)5-22(18,19)11-6-10(14)20-21(15,16)17/h1-4,11,14H,5-6H2,(H,12,13)(H2,15,16,17)
InChIKeySEUMVDPBYULKQH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6B(CNS(=O)(=O)Cc1cccc(c1)C(=O)O)(O)OP(=O)(O)O
CACTVS 3.385OB(CN[S](=O)(=O)Cc1cccc(c1)C(O)=O)O[P](O)(O)=O
ACDLabs 12.01c1ccc(CS(=O)(NCB(OP(O)(O)=O)O)=O)cc1C(O)=O
FormulaC9 H13 B N O9 P S
Name3-(5,7,7-trihydroxy-2,2,7-trioxo-6-oxa-2lambda~6~-thia-3-aza-7lambda~5~-phospha-5-boraheptan-1-yl)benzoic acid
ChEMBL
DrugBank
ZINC
PDB chain5wae Chain C Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5wae Structure-Based Analysis of Boronic Acids as Inhibitors of Acinetobacter-Derived Cephalosporinase-7, a Unique Class C beta-Lactamase.
Resolution1.804 Å
Binding residue
(original residue number in PDB)		S64 Y150 N213 Y222 T313 G314 S315 T316 S317
Binding residue
(residue number reindexed from 1)		S62 Y148 N211 Y220 T311 G312 S313 T314 S315
Annotation score1
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.
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

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5wae, PDBe:5wae, PDBj:5wae
PDBsum5wae
PubMed29144724
UniProtQ6DRA1

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