+Open data
-Basic information
Entry | Database: PDB / ID: 1fdj | ||||||
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Title | FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT LIVER | ||||||
Components | FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE | ||||||
Keywords | LYASE / ALDOLASE / LYASE (ALDEHYDE) / SCHIFF BASE / GLYCOLYSIS | ||||||
Function / homology | Function and homology information fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / microtubule organizing center / glycolytic process / cytoplasm Similarity search - Function | ||||||
Biological species | Oryctolagus cuniculus (rabbit) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.1 Å | ||||||
Authors | Blom, N.S. / White, A. / Sygusch, J. | ||||||
Citation | Journal: To be Published Title: Reaction intermediates of Rabbit liver D-fructose 1,6-bisphosphate Aldolase Authors: Blom, N.S. / White, A. / Sygusch, J. #1: Journal: Nat.Struct.Biol. / Year: 1997 Title: Product binding and role of the C-terminal region in Class-I D-fructose 1,6 bisphosphate Aldolase Authors: Blom, N.S. / Sygusch, J. #2: Journal: Acta Crystallogr.,Sect.D / Year: 1998 Title: Enhanced electron density envelopes by extended solvent definition Authors: Blom, N.S. / Sygusch, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fdj.cif.gz | 369.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fdj.ent.gz | 307 KB | Display | PDB format |
PDBx/mmJSON format | 1fdj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fdj_validation.pdf.gz | 514.9 KB | Display | wwPDB validaton report |
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Full document | 1fdj_full_validation.pdf.gz | 554 KB | Display | |
Data in XML | 1fdj_validation.xml.gz | 35.8 KB | Display | |
Data in CIF | 1fdj_validation.cif.gz | 72 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fd/1fdj ftp://data.pdbj.org/pub/pdb/validation_reports/fd/1fdj | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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Details | 2 half tetramers: one half tetramers is formed by chains A and B, the other half tetramer is formed by chains C and D |
-Components
-Protein / Sugars , 2 types, 6 molecules ABCD
#1: Protein | Mass: 39508.922 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / Organ: LIVER / References: UniProt: P79226, fructose-bisphosphate aldolase #3: Sugar | |
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-Non-polymers , 4 types, 3486 molecules
#2: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-13P / #5: Chemical | ChemComp-G3P / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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-Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 60.53 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 45% saturated ammonium sulphate solution, 100mM Tris.HCl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: XENTRONICS / Detector: AREA DETECTOR / Date: Nov 10, 1994 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.13→12 Å / Num. all: 100603 / Num. obs: 85613 / % possible obs: 85.1 % / Observed criterion σ(F): 1 / Observed criterion σ(I): -3 / Redundancy: 4.5 % / Biso Wilson estimate: 10 Å2 / Rmerge(I) obs: 0.092 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 2.13→2.25 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.18 / Num. unique all: 100603 / % possible all: 68.1 |
-Processing
Software |
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Refinement | Resolution: 2.1→12 Å / σ(F): 1 / σ(I): 1 / Stereochemistry target values: XPLOR parhcsdx
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Refinement step | Cycle: LAST / Resolution: 2.1→12 Å
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Refine LS restraints |
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