Structure of PDB 1fsy Chain A Binding Site BS01

Receptor Information
>1fsy Chain A (length=358) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALA
Ligand information
Ligand ID105
InChIInChI=1S/C12H12BClN2O4/c1-7-10(12(17)15-6-13(18)19)11(16-20-7)8-4-2-3-5-9(8)14/h2-5,18-19H,6H2,1H3,(H,15,17)
InChIKeyLSXNXXCBOPILJR-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0B(CNC(=O)c1c(onc1c2ccccc2Cl)C)(O)O
ACDLabs 10.04Clc1ccccc1c2noc(c2C(=O)NCB(O)O)C
CACTVS 3.341Cc1onc(c2ccccc2Cl)c1C(=O)NCB(O)O
FormulaC12 H12 B Cl N2 O4
NameN-[5-METHYL-3-O-TOLYL-ISOXAZOLE-4-CARBOXYLIC ACID AMIDE] BORONIC ACID;
CLOXACILLIN DERIVATIVE
ChEMBLCHEMBL324688
DrugBank
ZINC
PDB chain1fsy Chain A Residue 964 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1fsy Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases.
Resolution1.75 Å
Binding residue
(original residue number in PDB)		S64 Q120 Y150 N152 Y221 A318
Binding residue
(residue number reindexed from 1)		S61 Q117 Y147 N149 Y218 A315
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=6.82,Ki=0.15uM
BindingDB: Ki=150nM
Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 A114 V121 Y150 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 Y147 G153 E269 K312 A315
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
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fsy, PDBe:1fsy, PDBj:1fsy
PDBsum1fsy
PubMed11182316
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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