Structure of PDB 4e3n Chain A Binding Site BS01

Receptor Information
>4e3n 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
WQILNALQ
Ligand information
Ligand ID0NE
InChIInChI=1S/C9H9BF3N5O4S/c11-9(12,13)6-3-5(8-15-17-18-16-8)1-2-7(6)23(21,22)14-4-10(19)20/h1-3,14,19-20H,4H2,(H,15,16,17,18)
InChIKeyKJEUORQIESDSSV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=S(=O)(c2c(cc(c1nnnn1)cc2)C(F)(F)F)NCB(O)O
CACTVS 3.370OB(O)CN[S](=O)(=O)c1ccc(cc1C(F)(F)F)c2[nH]nnn2
OpenEye OEToolkits 1.7.6B(CNS(=O)(=O)c1ccc(cc1C(F)(F)F)c2[nH]nnn2)(O)O
FormulaC9 H9 B F3 N5 O4 S
Name[({[4-(1H-tetrazol-5-yl)-2-(trifluoromethyl)phenyl]sulfonyl}amino)methyl]boronic acid
ChEMBLCHEMBL3613796
DrugBank
ZINCZINC000205326991
PDB chain4e3n Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4e3n Fragment-guided design of subnanomolar beta-lactamase inhibitors active in vivo.
Resolution1.49 Å
Binding residue
(original residue number in PDB)		S64 Y150 V211 Y221 A318 T319 G320
Binding residue
(residue number reindexed from 1)		S61 Y147 V208 Y218 A315 T316 G317
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=10.30,Ki=0.05nM
BindingDB: Ki=50nM
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
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Biological Process
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Cellular Component
External links
PDB RCSB:4e3n, PDBe:4e3n, PDBj:4e3n
PDBsum4e3n
PubMed23043117
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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