Structure of PDB 1o9i Chain F

Receptor sequence
>1o9iF (length=266) Species: 1590 (Lactiplantibacillus plantarum) [Search protein sequence]
MFKHTRKLQYNAKPDRSDPIMARRLQESLGGQWGETTGMMSFLSQGWAST
GAEKYKDLLLDTGTEEMAHVEMISTMIGYLLEDAPFGPEDLKRDPSLATT
MAGMDPEHSLVHGLNASLNNPNGAAWNAGYVTSSGNLVADMRFNVVRESE
ARLQVSRLYSMTEDEGVRDMLKFLLARETQHQLQFMKAQEELEEKYGIIV
PGDMKEIEHSEFSHVLMNFSDGDGSKAFEGQVAKDGEKFTYQENPEAMGG
IPHIKPGDPRLHNHQG
3D structure
PDB1o9i Outer Sphere Mutagenesis of Lactobacillus Plantarum Manganese Catalase Disrupts the Cluster Core. Mechanistic Implications.
ChainF
Resolution1.33 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA F N218 S220 G222 N218 S220 G222
BS02 MN3 F E35 E66 H69 E35 E66 H69
BS03 MN3 F E66 E148 H181 E66 E148 H181
BS04 CA F D57 D61 D57 D61
BS05 O F E66 H69 H181 E66 H69 H181
Gene Ontology
Molecular Function
GO:0004096 catalase activity
GO:0004601 peroxidase activity
GO:0046872 metal ion binding
Biological Process
GO:0098869 cellular oxidant detoxification

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1o9i, PDBe:1o9i, PDBj:1o9i
PDBsum1o9i
PubMed12631270
UniProtP60355|MCAT_LACPN Manganese catalase

[Back to BioLiP]