Structure of PDB 7zo3 Chain A Binding Site BS02

Receptor Information
>7zo3 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 IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain7zo3 Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7zo3 Interactions of hydrolyzed beta-lactams with the L1 metallo-beta-lactamase: Crystallography supports stereoselective binding of cephem/carbapenem products.
Resolution1.43 Å
Binding residue
(original residue number in PDB)
H84 H86 H160
Binding residue
(residue number reindexed from 1)
H83 H85 H159
Annotation score1
Enzymatic activity
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:7zo3, PDBe:7zo3, PDBj:7zo3
PDBsum7zo3
PubMed36924941
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

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