Structure of PDB 1dxk Chain A Binding Site BS02

Receptor Information

>1dxk Chain A (length=221) Species: 1396 (Bacillus cereus)

TVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVD
SSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAH
STALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVV
WLPQYNILVGGSLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAV
VPGHGEVGDKGLLLHTLDLLK

Ligand information

• Ligand ID: BCT
• InChI: InChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-1
• InChIKey: BVKZGUZCCUSVTD-UHFFFAOYSA-M
• SMILES:
  OpenEye OEToolkits 1.5.0: C(=O)(O)[O-]
  CACTVS 3.341: OC([O-])=O
  ACDLabs 10.04: [O-]C(=O)O
• Formula: C H O3
• Name: BICARBONATE ION
• PDB chain: 1dxk Chain A Residue 230

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1dxk Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.
• Resolution: 1.85 Å
• Binding residue (original residue number in PDB): H149 S168
• Binding residue (residue number reindexed from 1): H143 S162
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H86 H88 D90 H149 S168 K171 N180 H210
• Catalytic site (residue number reindexed from 1): H80 H82 D84 H143 S162 K165 N174 H204
• 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:1dxk, PDBe:1dxk, PDBj:1dxk
• PDBsum: 1dxk
• PubMed: 10933508
• UniProt: P04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)