Structure of PDB 1xgj Chain A Binding Site BS01

Receptor Information
>1xgj Chain A (length=351) 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
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIIALAARPVKAITPPTPAVRA
SWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNAL
Q
Ligand information
Ligand IDHTC
InChIInChI=1S/C12H9NO7S2/c14-8-5-6(11(15)16)1-2-7(8)13-22(19,20)9-3-4-21-10(9)12(17)18/h1-5,13-14H,(H,15,16)(H,17,18)
InChIKeyRDPXXOOKKRIKFN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)c1sccc1[S](=O)(=O)Nc2ccc(cc2O)C(O)=O
ACDLabs 10.04O=C(O)c1sccc1S(=O)(=O)Nc2ccc(C(=O)O)cc2O
OpenEye OEToolkits 1.5.0c1cc(c(cc1C(=O)O)O)NS(=O)(=O)c2ccsc2C(=O)O
FormulaC12 H9 N O7 S2
Name3-{[(4-CARBOXY-2-HYDROXYANILINE]SULFONYL}THIOPHENE-2-CARBOXYLIC ACID
ChEMBLCHEMBL1222313
DrugBankDB07927
ZINCZINC000003881294
PDB chain1xgj Chain A Residue 777 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1xgj Structure-based optimization of a non-beta-lactam lead results in inhibitors that do not up-regulate beta-lactamase expression in cell culture.
Resolution1.97 Å
Binding residue
(original residue number in PDB)		S64 L119 N152 Y221 G317 A318 T319 G320
Binding residue
(residue number reindexed from 1)		S61 L116 N149 Y218 G307 A308 T309 G310
Annotation score1
Binding affinityMOAD: Ki=1uM
PDBbind-CN: -logKd/Ki=6.00,Ki=1.0uM
BindingDB: Ki=1000nM
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 K305 A308
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:1xgj, PDBe:1xgj, PDBj:1xgj
PDBsum1xgj
PubMed15796528
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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