Structure of PDB 2bfl Chain B Binding Site BS01

Receptor Information

>2bfl Chain B (length=220) Species: 1396 (Bacillus cereus)

KTVIKNETGTISISQLNKNVWVHTELGSFNAVPSNGLVLNTSKGLVLVDS
SWDDKLTKELIEMVEKKFQKRVTDVIITHAHADCIGGIKTLKERGIKAHS
TALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVW
LPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVV
PGHGEVGDKGLLLHTLDLLK

Ligand information

• Ligand ID: AZI
• InChI: InChI=1S/N3/c1-3-2/q-1
• InChIKey: IVRMZWNICZWHMI-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [N-]=[N+]=[N-]
• Formula: N3
• Name: AZIDE ION
• ChEMBL: CHEMBL79455
• PDB chain: 2bfl Chain B Residue 1295

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2bfl Effect of Ph on the Active Site of an Arg121Cys Mutant of the Metallo-Beta-Lactamase from Bacillus Cereus: Implications for the Enzyme Mechanism
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): H196 G232 N233
• Binding residue (residue number reindexed from 1): H142 G172 N173
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H116 H118 D120 H196 C221 K224 N233 H263
• Catalytic site (residue number reindexed from 1): H79 H81 D83 H142 C161 K164 N173 H203
• 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

External links

• PDB: RCSB:2bfl, PDBe:2bfl, PDBj:2bfl
• PDBsum: 2bfl
• PubMed: 15779910
• UniProt: P04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)