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Yorodumi- PDB-2fus: MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fus | ||||||
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Title | MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AND A NEARBY DICARBOXYLIC ACID BINDING SITE | ||||||
Components | FUMARASE C | ||||||
Keywords | HYDROLYASE / CARBON OXYGEN LYASE / KREB'S CYCLE ENZYME / FUMARATE HYDRATASE | ||||||
Function / homology | Function and homology information tricarboxylic acid cycle heteromeric enzyme complex / fumarate hydratase activity / fumarate hydratase / fumarate metabolic process / malate metabolic process / tricarboxylic acid cycle / response to oxidative stress / identical protein binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Weaver, T.M. / Lees, M. / Banaszak, L.J. | ||||||
Citation | Journal: Protein Sci. / Year: 1997 Title: Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Authors: Weaver, T. / Lees, M. / Banaszak, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fus.cif.gz | 229.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fus.ent.gz | 190.6 KB | Display | PDB format |
PDBx/mmJSON format | 2fus.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fu/2fus ftp://data.pdbj.org/pub/pdb/validation_reports/fu/2fus | HTTPS FTP |
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-Related structure data
Related structure data | 1furC 1fuoS 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.4695, -0.0031, 0.8829), Vector: |
-Components
#1: Protein | Mass: 50524.730 Da / Num. of mol.: 2 / Mutation: H129N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: JM105 / Cell line: 293 / Cellular location: CYTOPLASM / Gene: FUMC / Plasmid: PASK40_129EFUMC / Cellular location (production host): CYTOPLASM / Gene (production host): FUMC / Production host: Escherichia coli (E. coli) / References: UniProt: P05042, fumarate hydratase #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | THE SECOND ANION BINDING SITE LOCATED BETWEEN ARG 126 THROUGH ASN 135 HAS BEEN STERICALLY BLOCKED ...THE SECOND ANION BINDING SITE LOCATED BETWEEN ARG 126 THROUGH ASN 135 HAS BEEN STERICALLY | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50 % | |||||||||||||||
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Crystal grow | pH: 5 Details: PROTEIN WAS CRYSTALLIZED FROM 150MM CITRATE PH 5.0 AND 14% PEG 4000 | |||||||||||||||
Crystal grow | *PLUS pH: 6 / Method: unknown | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Feb 1, 1996 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.98→8 Å / Num. obs: 60762 / % possible obs: 88 % / Observed criterion σ(I): 1 / Redundancy: 4.3 % / Rmerge(I) obs: 0.07 / Rsym value: 0.117 / Net I/σ(I): 7.4 |
Reflection shell | Resolution: 1.98→2.06 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.61 / Mean I/σ(I) obs: 0.435 / Rsym value: 0.71 / % possible all: 46 |
Reflection shell | *PLUS % possible obs: 46 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FUO Resolution: 2.2→8 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 1
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Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.3 Å / Total num. of bins used: 8 / % reflection obs: 85.26 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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