+Open data
-Basic information
Entry | Database: PDB / ID: 1fui | ||||||
---|---|---|---|---|---|---|---|
Title | L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI | ||||||
Components | L-FUCOSE ISOMERASE | ||||||
Keywords | ISOMERASE / KETOL ISOMERASE / FUCOSE METABOLISM / L-FUCOSE TO L-FUCULOSE CONVERSION | ||||||
Function / homology | Function and homology information D-arabinose isomerase / arabinose isomerase activity / L-fucose isomerase / L-fucose isomerase activity / D-arabinose catabolic process / L-fucose catabolic process / manganese ion binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SINGLE ISOMORPHOUS REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Seemann, J.E. / Schulz, G.E. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1997 Title: Structure and mechanism of L-fucose isomerase from Escherichia coli. Authors: Seemann, J.E. / Schulz, G.E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1fui.cif.gz | 685.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1fui.ent.gz | 566.5 KB | Display | PDB format |
PDBx/mmJSON format | 1fui.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fui_validation.pdf.gz | 503.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1fui_full_validation.pdf.gz | 547.4 KB | Display | |
Data in XML | 1fui_validation.xml.gz | 128.1 KB | Display | |
Data in CIF | 1fui_validation.cif.gz | 177.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fu/1fui ftp://data.pdbj.org/pub/pdb/validation_reports/fu/1fui | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||||||||||
2 |
| ||||||||||||||||||||||||
3 |
| ||||||||||||||||||||||||
Unit cell |
| ||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
| ||||||||||||||||||||||||
Details | THE ASYMMETRIC UNIT CONTAINS TWO TRIMERS. |
-Components
#1: Protein | Mass: 65049.547 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Cell line: JM105 / Cellular location: CYTOPLASM / Gene: FUCI / Plasmid: PKK223-3 / Species (production host): Escherichia coli / Cell line (production host): JM105 / Cellular location (production host): CYTOPLASM / Gene (production host): FUCI / Production host: Escherichia coli K12 (bacteria) / Strain (production host): K12 / References: UniProt: P69922, D-arabinose isomerase #2: Chemical | ChemComp-MN / #3: Chemical | #4: Chemical | ChemComp-FOC / #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 4 |
---|
-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 7.5 Details: 2.01 M AMMONIUM SULFATE 2% PEG 400 1 MM MNCL2 10 MM 2-MERCAPTOETHANOL 10 MM L-FUCITOL 100 MM HEPES, PH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 293 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.92 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 118481 / % possible obs: 87 % / Observed criterion σ(I): 3 / Redundancy: 2.3 % / Biso Wilson estimate: 38 Å2 / Rsym value: 0.099 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 2.5→2.63 Å / Redundancy: 2 % / Mean I/σ(I) obs: 2.4 / Rsym value: 0.297 / % possible all: 82 |
Reflection | *PLUS Num. measured all: 273560 / Rmerge(I) obs: 0.099 |
Reflection shell | *PLUS % possible obs: 82.4 % / Rmerge(I) obs: 0.297 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: SINGLE ISOMORPHOUS REPLACEMENT Resolution: 2.5→20 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0 / Details: THE ASYMMETRIC UNIT CONTAINS TWO TRIMERS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å / Luzzati d res low obs: 4.4 Å / Luzzati sigma a obs: 0.26 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.5→2.59 Å / Rfactor Rfree error: 0.03 / Total num. of bins used: 10
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|