Structure of PDB 1jku Chain D Binding Site BS02

Receptor Information
>1jku Chain D (length=266) Species: 1590 (Lactiplantibacillus plantarum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFKHTRKLQYNAKPDRSDPIMARRLQESLGGQWGETTGMMSYLSQGWAST
GAEKYKDLLLDTGTEEMAHVEMISTMIGYLLEDAPFGPEDLKRDPSLATT
MAGMDPEHSLVHGLNASLNNPNGAAWNAGYVTSSGNLVADMRFNVVRESE
ARLQVSRLYSMTEDEGVRDMLKFLLARETQHQLQFMKAQEELEEKYGIIV
PGDMKEIEHSEFSHVLMNFSDGDGSKAFEGQVAKDGEKFTYQENPEAMGG
IPHIKPGDPRLHNHQG
Ligand information
Ligand IDMN3
InChIInChI=1S/Mn/q+3
InChIKeyMMIPFLVOWGHZQD-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Mn+3]
FormulaMn
NameMANGANESE (III) ION
ChEMBL
DrugBank
ZINC
PDB chain1jku Chain D Residue 4267 [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]
PDB1jku Crystal structure of manganese catalase from Lactobacillus plantarum.
Resolution1.84 Å
Binding residue
(original residue number in PDB)
E35 E66 H69
Binding residue
(residue number reindexed from 1)
E35 E66 H69
Annotation score1
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1jku, PDBe:1jku, PDBj:1jku
PDBsum1jku
PubMed11587647
UniProtP60355|MCAT_LACPN Manganese catalase

[Back to BioLiP]