Structure of PDB 2qjs Chain D Binding Site BS01

Receptor Information

>2qjs Chain D (length=248) Species: 40324 (Stenotrophomonas maltophilia)

PMAPLQIADHTWQIGTEDLTALLVQTPDGAVLLDGGMPQMASHLLDNMKA
RGVTPRDLRLILLSHAHANHAGPVAELKRRTGAKVAANAESAVLLARGGS
DDLHFGDGITYPPANADRIVMDGEVITVGGIVFTAHFMAGHTPGSTAWTW
TDTRNGKPVRIAYADSLSAPGYQLQGNPRYPHLIEDYRRSFATVRALPCD
VLLTPHPGASNWDYAAGARAGAKALTCKAYADAAEQKFDGQLAKETAG

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 2qjs Chain D Residue 2001

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2qjs Structural Basis for the Role of Asp-120 in Metallo-beta-lactamases
• Resolution: 2.25 Å
• Binding residue (original residue number in PDB): H121 H263
• Binding residue (residue number reindexed from 1): H70 H206
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H116 H118 N120 H121 H196 Y228 H263
• Catalytic site (residue number reindexed from 1): H65 H67 N69 H70 H141 Y172 H206
• 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

External links

• PDB: RCSB:2qjs, PDBe:2qjs, PDBj:2qjs
• PDBsum: 2qjs
• PubMed: 17715946
• UniProt: P52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3