Structure of PDB 3e1n Chain L

Receptor sequence
>3e1nL (length=156) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESID
EMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKN
LREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYL
QAQIRE
3D structure
PDB3e1n Structural basis for iron mineralization by bacterioferritin
ChainL
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.16.3.1: ferroxidase.
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 FE2 L E18 E51 H54 E127 E18 E51 H54 E127
BS02 FE2 L E51 E94 E127 H130 E51 E94 E127 H130
BS03 HEM L L19 I22 F26 Y45 I49 M52 L19 I22 F26 Y45 I49 M52
BS04 UNK L E51 E127 E51 E127
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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Cellular Component
External links
PDB RCSB:3e1n, PDBe:3e1n, PDBj:3e1n
PDBsum3e1n
PubMed19391621
UniProtP0ABD3|BFR_ECOLI Bacterioferritin (Gene Name=bfr)

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