Structure of PDB 4len Chain A Binding Site BS01

Receptor Information
>4len Chain A (length=263) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVM
AAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAA
ALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPG
DPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGL
PTSWTAGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRD
VLASAARIIAEGL
Ligand information
Ligand ID2GK
InChIInChI=1S/C11H9BO4S/c13-10(14)6-5-8-7-3-1-2-4-9(7)17-11(8)12(15)16/h1-6,15-16H,(H,13,14)/b6-5+
InChIKeyIYRVQPJBSDCZBO-AATRIKPKSA-N
SMILES
SoftwareSMILES
CACTVS 3.385OB(O)c1sc2ccccc2c1/C=C/C(O)=O
OpenEye OEToolkits 1.7.6B(c1c(c2ccccc2s1)C=CC(=O)O)(O)O
ACDLabs 12.01O=C(O)\C=C\c1c2ccccc2sc1B(O)O
OpenEye OEToolkits 1.7.6B(c1c(c2ccccc2s1)/C=C/C(=O)O)(O)O
CACTVS 3.385OB(O)c1sc2ccccc2c1C=CC(O)=O
FormulaC11 H9 B O4 S
Name(2E)-3-[2-(dihydroxyboranyl)-1-benzothiophen-3-yl]prop-2-enoic acid
ChEMBLCHEMBL3286879
DrugBank
ZINCZINC000221721124
PDB chain4len Chain A Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4len Targeting Class A and C Serine beta-Lactamases with a Broad-Spectrum Boronic Acid Derivative.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		C69 S70 N104 Y105 S130 N132 E166 N170 T235 G236 S237
Binding residue
(residue number reindexed from 1)		C44 S45 N79 Y80 S105 N107 E141 N145 T210 G211 S212
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.40,Ki=0.04uM
Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 S237
Catalytic site (residue number reindexed from 1) S45 K48 S105 E141 K209 S212
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:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4len, PDBe:4len, PDBj:4len
PDBsum4len
PubMed24882105
UniProtQ9L5C8

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