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Open data
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Basic information
Entry | Database: PDB / ID: 1bfr | ||||||
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Title | IRON STORAGE AND ELECTRON TRANSPORT | ||||||
![]() | BACTERIOFERRITIN | ||||||
![]() | ELECTRON TRANSPORT / IRON STORAGE | ||||||
Function / homology | ![]() ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / ferric iron binding / iron ion transport / oxidoreductase activity / iron ion binding / heme binding / protein homodimerization activity / identical protein binding ...ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / ferric iron binding / iron ion transport / oxidoreductase activity / iron ion binding / heme binding / protein homodimerization activity / identical protein binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Dautant, A. / Yariv, J. / Meyer, J.B. / Precigoux, G. / Sweet, R.M. / Frolow, F. / Kalb(Gilboa), A.J. | ||||||
![]() | ![]() Title: Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli. Authors: Dautant, A. / Meyer, J.B. / Yariv, J. / Precigoux, G. / Sweet, R.M. / Kalb, A.J. / Frolow, F. #1: ![]() Title: Structure of a Unique Twofold Symmetric Haem-Binding Site Authors: Frolow, F. / Kalb, A.J. / Yariv, J. #2: ![]() Title: A Crystallographic Study of Haem Binding to Ferritin Authors: Precigoux, G. / Yariv, J. / Gallois, B. / Dautant, A. / Courseille, C. / Langlois D'Estaintot, B. #3: ![]() Title: Amino Acid Sequence of the Bacterioferritin (Cytochrome B1) of Escherichia Coli-K12 Authors: Andrews, S.C. / Smith, J.M. / Guest, J.R. / Harrison, P.M. #4: ![]() Title: Molecular Size and Symmetry of the Bacterioferritin of Escherichia Coli. X-Ray Crystallographic Characterization of Four Crystal Forms Authors: Smith, J.M. / Ford, G.C. / Harrison, P.M. / Yariv, J. / Kalb, A.J. #5: ![]() Title: The Identity of Bacterioferritin and Cytochrome B1 Authors: Yariv, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 752.8 KB | Display | ![]() |
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PDB format | ![]() | 628.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 74.2 KB | Display | |
Data in CIF | ![]() | 96.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 18518.016 Da / Num. of mol.: 24 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | ChemComp-MN / #3: Chemical | ChemComp-HEM / Compound details | EACH SUBUNIT INCLUDES A BINUCLEAR METAL-BINDING SITE INVOLVING RESIDUES GLU 18, GLU 51, HIS 54, GLU ...EACH SUBUNIT INCLUDES A BINUCLEAR METAL-BINDING SITE INVOLVING RESIDUES GLU 18, GLU 51, HIS 54, GLU 94, GLU 127 AND HIS 130 AND LINKING TOGETHER THE FOUR MAJOR HELICES (A, B, C AND D) OF THE SUBUNIT. THE IDENTITY OF THE METAL IONS HAS NOT BEEN DETERMINED | Nonpolymer details | HEM IS POSITIONED BETWEEN TWO SUBUNITS WITH ITS QUASI TWO-FOLD AXIS NEARLY COINCIDING WITH A NON- ...HEM IS POSITIONED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.04 Å3/Da / Density % sol: 59.59 % | ||||||||||||||||||||||||
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Crystal grow | Details: THIS MONOCLINIC CRYSTAL WAS GROWN FROM A SOLUTION OF THE PROTEIN IN DISTILLED WATER BY THE ADDITION OF MN*CL2. | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: microdialysis | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.94 Å / Lowest resolution: 46.7 Å / Num. obs: 94076 / Rmerge(I) obs: 0.12 |
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Processing
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Refinement | Resolution: 2.94→10 Å / σ(F): 2 Details: THE STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT (PROGRAM *AMORE*) STARTING FROM THE COORDINATES IN PROTEIN DATA BANK ENTRY 1BCF OF BACTERIOFERRITIN IN HIGH SALT AND THE TETRAGONAL CRYSTAL ...Details: THE STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT (PROGRAM *AMORE*) STARTING FROM THE COORDINATES IN PROTEIN DATA BANK ENTRY 1BCF OF BACTERIOFERRITIN IN HIGH SALT AND THE TETRAGONAL CRYSTAL FORM. THE 11 NON-CRYSTALLOGRAPHIC TRANSFORMATIONS GIVEN IN THE *MTRIX* RECORDS WERE USED TO GENERATE THE COMPLETE ASYMMETRIC UNIT PRESENTED IN THIS ENTRY FROM THE COORDINATES PROVIDED BY THE DEPOSITORS. THE ASYMMETRIC UNIT CORRESPONDS TO 24 SUBUNITS AND 12 HEME MOLECULES AND THIS REPRESENTS A MOLECULE OF BACTERIOFERRITIN. STRONG ELECTRON DENSITY WAS OBSERVED ON THE FOUR-FOLD AXIS AT (X = 38.333, Y = 8.691, Z = 69.167). NO ATOM IS ASSIGNED TO THIS DENSITY UNTIL FURTHER EVIDENCE IS OBTAINED.
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Refinement step | Cycle: LAST / Resolution: 2.94→10 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection obs: 91554 / Rfactor obs: 0.22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 11 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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