Structure of PDB 1fsw Chain B Binding Site BS01

Receptor Information
>1fsw 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
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALA
Ligand information
Ligand IDCTB
InChIInChI=1S/C7H10BNO3S/c10-7(9-5-8(11)12)4-6-2-1-3-13-6/h1-3,11-12H,4-5H2,(H,9,10)
InChIKeyVXAPSUDMBNWYNC-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(NCB(O)O)Cc1sccc1
OpenEye OEToolkits 1.5.0B(CNC(=O)Cc1cccs1)(O)O
CACTVS 3.341OB(O)CNC(=O)Cc1sccc1
FormulaC7 H10 B N O3 S
NameN-2-THIOPHEN-2-YL-ACETAMIDE BORONIC ACID
ChEMBLCHEMBL320049
DrugBankDB02094
ZINC
PDB chain1fsw Chain B Residue 964 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1fsw Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		S64 K67 Q120 Y150 N152 A318 T319
Binding residue
(residue number reindexed from 1)		S61 K64 Q117 Y147 N149 A315 T316
Annotation score1
Binding affinityBindingDB: Ki=3.2e+2nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fsw, PDBe:1fsw, PDBj:1fsw
PDBsum1fsw
PubMed11182316
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

[Back to BioLiP]