Structure of PDB 1l2s Chain A Binding Site BS02

Receptor Information
>1l2s Chain A (length=355) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNLAARPVKAITPPTP
AVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQI
LNALQ
Ligand information
Ligand IDSTC
InChIInChI=1S/C11H8ClNO4S2/c12-7-1-3-8(4-2-7)13-19(16,17)9-5-6-18-10(9)11(14)15/h1-6,13H,(H,14,15)
InChIKeyYRWKEEDITQJPCZ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(ccc1NS(=O)(=O)c2ccsc2C(=O)O)Cl
CACTVS 3.341OC(=O)c1sccc1[S](=O)(=O)Nc2ccc(Cl)cc2
ACDLabs 10.04O=C(O)c1sccc1S(=O)(=O)Nc2ccc(Cl)cc2
FormulaC11 H8 Cl N O4 S2
Name3-[(4-CHLOROANILINO)SULFONYL]THIOPHENE-2-CARBOXYLIC ACID
ChEMBLCHEMBL372227
DrugBankDB08573
ZINCZINC000000116295
PDB chain1l2s Chain B Residue 3115 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1l2s Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase.
Resolution1.94 Å
Binding residue
(original residue number in PDB)		A79 Q250 L254 S257 P306
Binding residue
(residue number reindexed from 1)		A76 Q247 L251 S254 P300
Annotation score1
Binding affinityMOAD: Ki=26uM
PDBbind-CN: -logKd/Ki=4.59,Ki=26uM
BindingDB: Ki=26000nM
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 K309 A312
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:1l2s, PDBe:1l2s, PDBj:1l2s
PDBsum1l2s
PubMed12121656
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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