Structure of PDB 5evd Chain A Binding Site BS01

Receptor Information
>5evd Chain A (length=267) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AEVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAV
LLDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRT
GAKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGI
VFTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYP
HLIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYA
DAAEQKFDGQLAKETAG
Ligand information
Ligand IDVC2
InChIInChI=1S/C9H15NO2S3/c1-9(2)7(8(11)12)10-5(3-13)14-4-6(10)15-9/h5-7,13H,3-4H2,1-2H3,(H,11,12)/t5-,6+,7-/m0/s1
InChIKeyIKSIYRPSHTUWIX-XVMARJQXSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6CC1(C(N2C(S1)CSC2CS)C(=O)O)C
OpenEye OEToolkits 1.7.6CC1([C@@H](N2[C@H](S1)CS[C@H]2CS)C(=O)O)C
CACTVS 3.385CC1(C)S[CH]2CS[CH](CS)N2[CH]1C(O)=O
CACTVS 3.385CC1(C)S[C@@H]2CS[C@@H](CS)N2[C@H]1C(O)=O
ACDLabs 12.01O=C(O)C1N2C(SCC2SC1(C)C)CS
FormulaC9 H15 N O2 S3
Name(3S,5S,7aR)-2,2-dimethyl-5-(sulfanylmethyl)tetrahydro[1,3]thiazolo[4,3-b][1,3]thiazole-3-carboxylic acid
ChEMBLCHEMBL5176024
DrugBank
ZINCZINC000219081868
PDB chain5evd Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5evd Cross-class metallo-beta-lactamase inhibition by bisthiazolidines reveals multiple binding modes.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		H118 D120 F156 I162 H196 P227
Binding residue
(residue number reindexed from 1)		H86 D88 F124 I128 H160 P189
Annotation score1
Binding affinityMOAD: Ki=10uM
PDBbind-CN: -logKd/Ki=5.00,Ki=10uM
Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 D120 H121 H196 Y229 H263
Catalytic site (residue number reindexed from 1) H84 H86 D88 H89 H160 Y191 H225
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:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0042597 periplasmic space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5evd, PDBe:5evd, PDBj:5evd
PDBsum5evd
PubMed27303030
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

[Back to BioLiP]