Structure of PDB 1bfr Chain T

Receptor sequence
>1bfrT (length=158) Species: 562 (Escherichia coli) [Search protein sequence]
MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESID
EMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKN
LREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYL
QAQIREEG
3D structure
PDB1bfr Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli.
ChainT
Resolution2.94 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MN T E51 E94 E127 H130 E51 E94 E127 H130
BS02 MN T E18 E51 H54 E127 E18 E51 H54 E127
BS03 HEM T I22 F26 I49 M52 I22 F26 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

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

[Back to BioLiP]