Structure of PDB 1pi4 Chain A Binding Site BS01

Receptor Information
>1pi4 Chain A (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
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDAKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ
Ligand information
Ligand IDSM3
InChIInChI=1S/C13H14BNO3S/c16-12(9-11-7-4-8-19-11)15-13(14(17)18)10-5-2-1-3-6-10/h1-8,13,17-18H,9H2,(H,15,16)/t13-/m0/s1
InChIKeyLGJCDEZMANATFA-ZDUSSCGKSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0B(C(c1ccccc1)NC(=O)Cc2cccs2)(O)O
ACDLabs 10.04O=C(NC(B(O)O)c1ccccc1)Cc2sccc2
CACTVS 3.341OB(O)[C@@H](NC(=O)Cc1sccc1)c2ccccc2
OpenEye OEToolkits 1.5.0B([C@H](c1ccccc1)NC(=O)Cc2cccs2)(O)O
CACTVS 3.341OB(O)[CH](NC(=O)Cc1sccc1)c2ccccc2
FormulaC13 H14 B N O3 S
Name(1R)-1-(2-THIENYLACETYLAMINO)-1-PHENYLMETHYLBORONIC ACID
ChEMBLCHEMBL404155
DrugBankDB08552
ZINCZINC000169748509
PDB chain1pi4 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1pi4 Thermodynamic cycle analysis and inhibitor design against beta-lactamase.
Resolution1.39 Å
Binding residue
(original residue number in PDB)		S64 L119 Y150 Y221 G317 A318 T319 G320
Binding residue
(residue number reindexed from 1)		S61 L116 Y147 Y218 G314 A315 T316 G317
Annotation score1
Binding affinityMOAD: Ki=37nM
PDBbind-CN: -logKd/Ki=7.43,Ki=37nM
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:1pi4, PDBe:1pi4, PDBj:1pi4
PDBsum1pi4
PubMed14661960
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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