Structure of PDB 1o9i Chain B Binding Site BS02
Receptor Information
>1o9i Chain B (length=266) Species:
1590
(Lactiplantibacillus plantarum) [
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MFKHTRKLQYNAKPDRSDPIMARRLQESLGGQWGETTGMMSFLSQGWAST
GAEKYKDLLLDTGTEEMAHVEMISTMIGYLLEDAPFGPEDLKRDPSLATT
MAGMDPEHSLVHGLNASLNNPNGAAWNAGYVTSSGNLVADMRFNVVRESE
ARLQVSRLYSMTEDEGVRDMLKFLLARETQHQLQFMKAQEELEEKYGIIV
PGDMKEIEHSEFSHVLMNFSDGDGSKAFEGQVAKDGEKFTYQENPEAMGG
IPHIKPGDPRLHNHQG
Ligand information
Ligand ID
MN3
InChI
InChI=1S/Mn/q+3
InChIKey
MMIPFLVOWGHZQD-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Mn+3]
Formula
Mn
Name
MANGANESE (III) ION
ChEMBL
DrugBank
ZINC
PDB chain
1o9i Chain B Residue 268 [
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Receptor-Ligand Complex Structure
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PDB
1o9i
Outer Sphere Mutagenesis of Lactobacillus Plantarum Manganese Catalase Disrupts the Cluster Core. Mechanistic Implications.
Resolution
1.33 Å
Binding residue
(original residue number in PDB)
E66 E148 H181
Binding residue
(residue number reindexed from 1)
E66 E148 H181
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
E35 E66 H69 E148 E178 H181
Catalytic site (residue number reindexed from 1)
E35 E66 H69 E148 E178 H181
Enzyme Commision number
1.11.1.6
: catalase.
Gene Ontology
Molecular Function
GO:0004096
catalase activity
GO:0004601
peroxidase activity
GO:0046872
metal ion binding
Biological Process
GO:0098869
cellular oxidant detoxification
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Molecular Function
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Biological Process
External links
PDB
RCSB:1o9i
,
PDBe:1o9i
,
PDBj:1o9i
PDBsum
1o9i
PubMed
12631270
UniProt
P60355
|MCAT_LACPN Manganese catalase
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