+Open data
-Basic information
Entry | Database: PDB / ID: 2fg4 | ||||||
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Title | Structure of Human Ferritin L Chain | ||||||
Components | Ferritin light chain | ||||||
Keywords | METAL BINDING PROTEIN / Human Light Chain Ferritin | ||||||
Function / homology | Function and homology information : / autolysosome / Scavenging by Class A Receptors / Golgi Associated Vesicle Biogenesis / intracellular sequestering of iron ion / ferric iron binding / ferrous iron binding / Iron uptake and transport / azurophil granule lumen / iron ion transport ...: / autolysosome / Scavenging by Class A Receptors / Golgi Associated Vesicle Biogenesis / intracellular sequestering of iron ion / ferric iron binding / ferrous iron binding / Iron uptake and transport / azurophil granule lumen / iron ion transport / intracellular iron ion homeostasis / iron ion binding / Neutrophil degranulation / extracellular exosome / extracellular region / membrane / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Wang, Z. / Li, C. / Ellenburg, M. / Ruble, J. / Ho, J.X. / Carter, D.C. | ||||||
Citation | Journal: ACTA CRYSTALLOGR.,SECT.D / Year: 2006 Title: Structure of human ferritin L chain. Authors: Wang, Z. / Li, C. / Ellenburg, M. / Soistman, E. / Ruble, J. / Wright, B. / Ho, J.X. / Carter, D.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fg4.cif.gz | 53.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fg4.ent.gz | 38.2 KB | Display | PDB format |
PDBx/mmJSON format | 2fg4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fg/2fg4 ftp://data.pdbj.org/pub/pdb/validation_reports/fg/2fg4 | HTTPS FTP |
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-Related structure data
Related structure data | 2ffxSC 2fg8C S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 19917.486 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FTL / Plasmid: pET 11a-LF / Production host: Escherichia coli (E. coli) / References: UniProt: P02792 | ||
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#2: Chemical | ChemComp-CD / #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.74 Å3/Da / Density % sol: 67.07 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion / pH: 5 Details: 1.6% Cadmium Sulfate, 0.2M Sodium Acetate, pH 5.0, VAPOR DIFFUSION, temperature 294K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54178 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Dec 16, 2003 / Details: Osmic Blue |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. obs: 18119 / % possible obs: 96.1 % / Observed criterion σ(F): 1 / Biso Wilson estimate: 16.9 Å2 / Rsym value: 0.102 / Net I/σ(I): 15.5 |
Reflection shell | Highest resolution: 2.1 Å / % possible all: 96.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 2FFX Resolution: 2.1→24.8 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 469694.4 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 47.5883 Å2 / ksol: 0.347391 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.1→24.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.23 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 6
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Xplor file |
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