Structure of PDB 1li0 Chain A Binding Site BS01
Receptor Information
>1li0 Chain A (length=263) Species:
562
(Escherichia coli) [
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HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMISTFKVL
LCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSA
AITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPN
DERDTTTPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL
PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNR
QIAEIGASLIKHW
Ligand information
Ligand ID
BCT
InChI
InChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-1
InChIKey
BVKZGUZCCUSVTD-UHFFFAOYSA-M
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
C(=O)(O)[O-]
CACTVS 3.341
OC([O-])=O
ACDLabs 10.04
[O-]C(=O)O
Formula
C H O3
Name
BICARBONATE ION
ChEMBL
DrugBank
ZINC
PDB chain
1li0 Chain A Residue 1 [
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Receptor-Ligand Complex Structure
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PDB
1li0
The structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34.
Resolution
1.61 Å
Binding residue
(original residue number in PDB)
S130 A237
Binding residue
(residue number reindexed from 1)
S105 A212
Annotation score
1
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:1li0
,
PDBe:1li0
,
PDBj:1li0
PDBsum
1li0
PubMed
12058046
UniProt
P62593
|BLAT_ECOLX Beta-lactamase TEM (Gene Name=bla)
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