Structure of PDB 1ga9 Chain B Binding Site BS01

Receptor Information
>1ga9 Chain B (length=352) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYAKKQPVTQ
QTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGITL
LHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIG
LFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYRAV
HVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRY
WQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITPPTPAVR
ASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNA
LQ
Ligand information
Ligand IDETP
InChIInChI=1S/C16H14BNO6S3/c19-17(20)12-5-4-6-13(9-12)18-27(23,24)16-10-15(11-25-16)26(21,22)14-7-2-1-3-8-14/h1-11,18-20H
InChIKeyYZOKHYPIQNIFRQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OB(O)c1cccc(N[S](=O)(=O)c2scc(c2)[S](=O)(=O)c3ccccc3)c1
ACDLabs 10.04O=S(=O)(c1csc(c1)S(=O)(=O)Nc2cccc(B(O)O)c2)c3ccccc3
OpenEye OEToolkits 1.5.0B(c1cccc(c1)NS(=O)(=O)c2cc(cs2)S(=O)(=O)c3ccccc3)(O)O
FormulaC16 H14 B N O6 S3
Name3-(4-BENZENESULFONYL-THIOPHENE-2-SULFONYLAMINO)-PHENYLBORONIC ACID
ChEMBLCHEMBL113381
DrugBankDB02858
ZINCZINC000169748478
PDB chain1ga9 Chain B Residue 964 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ga9 Structure-based design and in-parallel synthesis of inhibitors of AmpC beta-lactamase.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		S64 Y150 N152 Y221 G317 A318 T319
Binding residue
(residue number reindexed from 1)		S58 Y144 N146 Y212 G308 A309 T310
Annotation score1
Binding affinityBindingDB: Ki=80nM
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) S58 K61 Y106 A108 V115 Y144 G150 E263 K306 A309
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:1ga9, PDBe:1ga9, PDBj:1ga9
PDBsum1ga9
PubMed11410378
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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