Structure of PDB 1bs3 Chain B Binding Site BS01

Receptor Information
>1bs3 Chain B (length=201) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AVYTLPELPYDYSALEPYISGEIMELHHDKHHKAYVDGANTALDKLAEAR
DKADFGAINKLEKDLAFNLAGHVNHSVFWKNMAPKGSAPERPTDELGAAI
DEFFGSFDNMKAQFTAAATGIQGSGWASLVWDPLGKRINTLQFYDHQNNL
PAGSIPLLQLDMWEHAFYLQYKNVKGDYVKSWWNVVNWDDVALRFSEARV
A
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain1bs3 Chain B Residue 202 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1bs3 Manipulating the coordination mumber of the ferric iron within the cambialistic superoxide dismutase of Propionibacterium shermanii by changing the pH-value A crystallographic analysis
Resolution1.55 Å
Binding residue
(original residue number in PDB)
H27 H75 D161 H165
Binding residue
(residue number reindexed from 1)
H27 H75 D161 H165
Annotation score1
Enzymatic activity
Enzyme Commision number 1.15.1.1: superoxide dismutase.
Gene Ontology
Molecular Function
GO:0004784 superoxide dismutase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006801 superoxide metabolic process
GO:0019430 removal of superoxide radicals

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1bs3, PDBe:1bs3, PDBj:1bs3
PDBsum1bs3
PubMed10231372
UniProtP80293|SODM_PROFR Superoxide dismutase [Mn/Fe] (Gene Name=sodA)

[Back to BioLiP]