Structure of PDB 1erm Chain A Binding Site BS01

Receptor Information
>1erm 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]
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVL
LCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSA
AITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPN
DERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL
PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNR
QIAEIGASLIKHW
Ligand information
Ligand IDBJI
InChIInChI=1S/C11H14BNO5/c1-7(14)13-10(12(17)18)6-8-3-2-4-9(5-8)11(15)16/h2-5,10,17-18H,6H2,1H3,(H,13,14)(H,15,16)/t10-/m0/s1
InChIKeyOBZSRKUYUGJGIM-JTQLQIEISA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(=O)N[CH](Cc1cccc(c1)C(O)=O)B(O)O
OpenEye OEToolkits 1.5.0B(C(Cc1cccc(c1)C(=O)O)NC(=O)C)(O)O
CACTVS 3.341CC(=O)N[C@@H](Cc1cccc(c1)C(O)=O)B(O)O
OpenEye OEToolkits 1.5.0B([C@H](Cc1cccc(c1)C(=O)O)NC(=O)C)(O)O
ACDLabs 10.04O=C(O)c1cc(ccc1)CC(NC(=O)C)B(O)O
FormulaC11 H14 B N O5
Name1(R)-1-ACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACID
ChEMBLCHEMBL1231367
DrugBankDB02614
ZINCZINC000169748475
PDB chain1erm Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1erm Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 beta-Lactamase(,).
Resolution1.7 Å
Binding residue
(original residue number in PDB)		M69 S70 S130 N132 E166 N170 S235 G236 A237
Binding residue
(residue number reindexed from 1)		M44 S45 S105 N107 E141 N145 S210 G211 A212
Annotation score1
Binding affinityBindingDB: Ki=110nM
Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 A237
Catalytic site (residue number reindexed from 1) S45 K48 S105 E141 K209 A212
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:1erm, PDBe:1erm, PDBj:1erm
PDBsum1erm
PubMed10820001
UniProtP62593|BLAT_ECOLX Beta-lactamase TEM (Gene Name=bla)

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