Structure of PDB 3ixg Chain B Binding Site BS01

Receptor Information
>3ixg Chain B (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
VTQQTLFELGSVSKTFIGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ
Ligand information
Ligand IDBZB
InChIInChI=1S/C8H7BO2S/c10-9(11)8-5-6-3-1-2-4-7(6)12-8/h1-5,10-11H
InChIKeyYNCYPMUJDDXIRH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0B(c1cc2ccccc2s1)(O)O
CACTVS 3.341OB(O)c1sc2ccccc2c1
ACDLabs 10.04OB(O)c2sc1ccccc1c2
FormulaC8 H7 B O2 S
NameBENZO[B]THIOPHENE-2-BORONIC ACID
ChEMBLCHEMBL34964
DrugBankDB04360
ZINCZINC000169743221
PDB chain3ixg Chain B Residue 362 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3ixg Structural bases for stability-function tradeoffs in antibiotic resistance.
Resolution2.14 Å
Binding residue
(original residue number in PDB)		S64 L119 Q120 Y150 N152 Y221 A318
Binding residue
(residue number reindexed from 1)		S61 L116 Q117 Y147 N149 Y218 A315
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.57,Ki=27nM
BindingDB: IC50=200nM,Ki=27nM
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:3ixg, PDBe:3ixg, PDBj:3ixg
PDBsum3ixg
PubMed19913034
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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