Structure of PDB 4tyt Chain A Binding Site BS03

Receptor Information
>4tyt Chain A (length=218) Species: 1396 (Bacillus cereus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EKTVIKNTGTISISQLNKNVWVHTELGSAVPSNGLVLNTSKGLVLVDSSW
DDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTA
LTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLP
QYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPG
HGEVGDKGLLLHTLDLLK
Ligand information
Ligand IDS3C
InChIInChI=1S/C9H5Cl3O2S/c10-5-1-2-6(11)8(12)4(5)3-7(15)9(13)14/h1-3,15H,(H,13,14)/b7-3-
InChIKeyZCOCHUAGSBNGCP-CLTKARDFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1cc(c(c(c1Cl)C=C(C(=O)O)S)Cl)Cl
CACTVS 3.385OC(=O)C(S)=Cc1c(Cl)ccc(Cl)c1Cl
CACTVS 3.385OC(=O)\C(S)=C\c1c(Cl)ccc(Cl)c1Cl
OpenEye OEToolkits 1.7.6c1cc(c(c(c1Cl)/C=C(/C(=O)O)\S)Cl)Cl
ACDLabs 12.01Clc1c(\C=C(/S)C(=O)O)c(Cl)ccc1Cl
FormulaC9 H5 Cl3 O2 S
Name(2Z)-2-sulfanyl-3-(2,3,6-trichlorophenyl)prop-2-enoic acid
ChEMBLCHEMBL3792857
DrugBank
ZINCZINC000214000735
PDB chain4tyt Chain A Residue 303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4tyt Rhodanine hydrolysis leads to potent thioenolate mediated metallo-beta-lactamase inhibition.
Resolution1.799 Å
Binding residue
(original residue number in PDB)		W89 H118 D120 H179 C198 N210 H240
Binding residue
(residue number reindexed from 1)		W50 H79 D81 H140 C159 N171 H201
Annotation score1
Binding affinityMOAD: ic50=0.02uM
PDBbind-CN: -logKd/Ki=7.70,IC50=0.02uM
BindingDB: IC50=80nM
Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 D120 H179 C198 K201 N210 H240
Catalytic site (residue number reindexed from 1) H77 H79 D81 H140 C159 K162 N171 H201
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
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:4tyt, PDBe:4tyt, PDBj:4tyt
PDBsum4tyt
PubMed25411887
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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