Structure of PDB 5evb Chain A Binding Site BS03

Receptor Information
>5evb Chain A (length=266) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVL
LDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRTG
AKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIV
FTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPH
LIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYAD
AAEQKFDGQLAKETAG
Ligand information
Ligand ID3R9
InChIInChI=1S/C7H11NO2S3/c9-7(10)4-2-12-6-3-13-5(1-11)8(4)6/h4-6,11H,1-3H2,(H,9,10)/t4-,5+,6-/m1/s1
InChIKeyZTWVMVSSSBGFHH-NGJCXOISSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C1C(N2C(S1)CSC2CS)C(=O)O
CACTVS 3.385OC(=O)[C@H]1CS[C@@H]2CS[C@@H](CS)N12
ACDLabs 12.01O=C(O)C1N2C(SCC2SC1)CS
CACTVS 3.385OC(=O)[CH]1CS[CH]2CS[CH](CS)N12
OpenEye OEToolkits 1.7.6C1[C@@H](N2[C@H](S1)CS[C@H]2CS)C(=O)O
FormulaC7 H11 N O2 S3
Name(3S,5S,7aR)-5-(sulfanylmethyl)tetrahydro[1,3]thiazolo[4,3-b][1,3]thiazole-3-carboxylic acid
ChEMBLCHEMBL5267944
DrugBank
ZINCZINC000219081771
PDB chain5evb Chain A Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5evb Cross-class metallo-beta-lactamase inhibition by bisthiazolidines reveals multiple binding modes.
Resolution1.841 Å
Binding residue
(original residue number in PDB)		H118 D120 F156 I162 H196 P227
Binding residue
(residue number reindexed from 1)		H85 D87 F123 I127 H159 P188
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) H83 H85 D87 H88 H159 Y190 H224
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5evb, PDBe:5evb, PDBj:5evb
PDBsum5evb
PubMed27303030
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

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