Structure of PDB 3e1p Chain J

Receptor sequence
>3e1pJ (length=158) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESID
EMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKN
LREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYL
QAQIREEG
3D structure
PDB3e1p Structural basis for iron mineralization by bacterioferritin
ChainJ
Resolution2.4 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 ZN J E18 E51 H54 E127 E18 E51 H54 E127
BS02 ZN J E51 E94 E127 H130 E51 E94 E127 H130
BS03 FE2 J H46 D50 H46 D50
BS04 HEM J L19 I22 F26 Y45 I49 M52 L19 I22 F26 Y45 I49 M52
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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Cellular Component
External links
PDB RCSB:3e1p, PDBe:3e1p, PDBj:3e1p
PDBsum3e1p
PubMed19391621
UniProtP0ABD3|BFR_ECOLI Bacterioferritin (Gene Name=bfr)

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