Structure of PDB 1mmm Chain B Binding Site BS01

Receptor Information
>1mmm Chain B (length=205) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFAN
LPVEELITKLDQLPADKKTVLRNNAGGHANHSLFWKGLKKGTTLQGDLKA
AIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPL
MGEAISGASGFPIMGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAAR
FAAKK
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 chain1mmm Chain B Residue 206 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1mmm Distinct Metal Environment in Fe-Substituted Manganese Superoxide Dismutase Provides a Structural Basis of Metal Specificity
Resolution2.2 Å
Binding residue
(original residue number in PDB)		H26 H81 D167 H171
Binding residue
(residue number reindexed from 1)		H26 H81 D167 H171
Annotation score1
Enzymatic activity
Enzyme Commision number 1.15.1.1: superoxide dismutase.
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0004784 superoxide dismutase activity
GO:0016209 antioxidant activity
GO:0016491 oxidoreductase activity
GO:0030145 manganese ion binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006801 superoxide metabolic process
GO:0006979 response to oxidative stress
GO:0009408 response to heat
GO:0010447 response to acidic pH
GO:0019430 removal of superoxide radicals
GO:0071291 cellular response to selenium ion
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1mmm, PDBe:1mmm, PDBj:1mmm
PDBsum1mmm
PubMed
UniProtP00448|SODM_ECOLI Superoxide dismutase [Mn] (Gene Name=sodA)

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