Structure of PDB 4jxv Chain B Binding Site BS01

Receptor Information
>4jxv 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
WQILNALQ
Ligand information
Ligand ID1MU
InChIInChI=1S/C14H13NO6S2/c16-13(17)10-3-1-9(2-4-10)5-7-15-23(20,21)11-6-8-22-12(11)14(18)19/h1-4,6,8,15H,5,7H2,(H,16,17)(H,18,19)
InChIKeyBTTJFJNWZFKJAU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370OC(=O)c1ccc(CCN[S](=O)(=O)c2ccsc2C(O)=O)cc1
ACDLabs 12.01O=S(=O)(c1c(scc1)C(=O)O)NCCc2ccc(C(=O)O)cc2
OpenEye OEToolkits 1.7.6c1cc(ccc1CCNS(=O)(=O)c2ccsc2C(=O)O)C(=O)O
FormulaC14 H13 N O6 S2
Name3-{[2-(4-carboxyphenyl)ethyl]sulfamoyl}thiophene-2-carboxylic acid
ChEMBLCHEMBL3287789
DrugBank
ZINCZINC000098207993
PDB chain4jxv Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4jxv Structure-based efforts to optimize a non-beta-lactam inhibitor of AmpC beta-lactamase.
Resolution1.76 Å
Binding residue
(original residue number in PDB)		S64 R204 G317 A318 T319 G320 N343
Binding residue
(residue number reindexed from 1)		S61 R201 G314 A315 T316 G317 N340
Annotation score1
Binding affinityMOAD: Ki=31uM
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
View graph for
Cellular Component
External links
PDB RCSB:4jxv, PDBe:4jxv, PDBj:4jxv
PDBsum4jxv
PubMed24835785
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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