Structure of PDB 1xgi Chain B Binding Site BS01

Receptor Information
>1xgi Chain B (length=358) 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
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ
Ligand information
Ligand IDNST
InChIInChI=1S/C11H8N2O6S2/c14-11(15)10-9(4-5-20-10)21(18,19)12-7-2-1-3-8(6-7)13(16)17/h1-6,12H,(H,14,15)
InChIKeyCITCNTPVKZFUAJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(cc(c1)[N+](=O)[O-])NS(=O)(=O)c2ccsc2C(=O)O
CACTVS 3.341OC(=O)c1sccc1[S](=O)(=O)Nc2cccc(c2)[N+]([O-])=O
ACDLabs 10.04O=C(O)c1sccc1S(=O)(=O)Nc2cccc([N+]([O-])=O)c2
FormulaC11 H8 N2 O6 S2
Name3-{[(3-NITROANILINE]SULFONYL}THIOPHENE-2-CARBOXYLIC ACID
ChEMBL
DrugBankDB08306
ZINCZINC000003881295
PDB chain1xgi Chain B Residue 416 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1xgi Structure-based optimization of a non-beta-lactam lead results in inhibitors that do not up-regulate beta-lactamase expression in cell culture.
Resolution1.96 Å
Binding residue
(original residue number in PDB)		S64 Q120 N152 Y221 G317 A318 T319 G320
Binding residue
(residue number reindexed from 1)		S61 Q117 N149 Y218 G314 A315 T316 G317
Annotation score1
Binding affinityMOAD: Ki=14uM
PDBbind-CN: -logKd/Ki=4.85,Ki=14uM
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:1xgi, PDBe:1xgi, PDBj:1xgi
PDBsum1xgi
PubMed15796528
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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