Structure of PDB 1bfr Chain B Binding Site BS01

Receptor Information
>1bfr Chain B (length=158) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESID
EMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKN
LREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYL
QAQIREEG
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1bfr Chain B Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1bfr Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli.
Resolution2.94 Å
Binding residue
(original residue number in PDB)		E51 E94 E127 H130
Binding residue
(residue number reindexed from 1)		E51 E94 E127 H130
Annotation score1
Enzymatic activity
Enzyme Commision number 1.16.3.1: ferroxidase.
Gene Ontology
Molecular Function
GO:0004322 ferroxidase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008199 ferric iron binding
GO:0015093 ferrous iron transmembrane transporter activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0140315 iron ion sequestering activity
Biological Process
GO:0006826 iron ion transport
GO:0006879 intracellular iron ion homeostasis
GO:0006880 intracellular sequestering of iron ion
GO:0034755 iron ion transmembrane transport
Cellular Component
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1bfr, PDBe:1bfr, PDBj:1bfr
PDBsum1bfr
PubMed9867433
UniProtP0ABD3|BFR_ECOLI Bacterioferritin (Gene Name=bfr)

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