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Open data
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Basic information
Entry | Database: PDB / ID: 1fuq | ||||||
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Title | FUMARASE WITH BOUND 3-TRIMETHYLSILYLSUCCINIC ACID | ||||||
![]() | FUMARASE C | ||||||
![]() | LYASE / TRICARBOXYLIC ACID CYCLE | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Weaver, T. / Banaszak, L. | ||||||
![]() | ![]() Title: Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Authors: Weaver, T. / Banaszak, L. #1: ![]() Title: The Multisubunit Active Site of Fumarase C from Escherichia Coli Authors: Weaver, T.M. / Levitt, D.G. / Donnelly, M.I. / Stevens, P.P. / Banaszak, L.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 | ![]() | 189.5 KB | Display | ![]() |
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PDB format | ![]() | 151.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 407.9 KB | Display | ![]() |
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Full document | ![]() | 425.8 KB | Display | |
Data in XML | ![]() | 20.8 KB | Display | |
Data in CIF | ![]() | 32.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Details | TWO SUBUNITS OF FUMARASE C ARE PRESENT IN THE ASU. THE MOLECULE IS A TETRAMER AND TRANSFORMATION MATRIX/VECTOR FOR GENERATING THE OTHER 2 SUBUNITS IS GIVEN. IN ONE SUBUNIT RESIDUES 317 - 320 ARE MISSING DUE TO A BREAK IN THE ELECTRON DENSITY. ALTHOUGH THIS IS A RECOMBINANT PROTEIN WITH A FIVE HISTIDINE ARM ON THE C-TERMINAL, NO ELECTRON DENSITY WAS SEEN TO ACCOUNT FOR THESE RESIDUES. THE CRYSTALLINE PROTEIN INCLUDES COORDINATES FOR A MALATE AND TRMETHYLSILYL MALEATE OBSERVED IN THE ELECTRON DENSITY AND DESCRIBED FULLY IN THE BIOCHEMISTRY REFERENCE. |
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Components
#1: Protein | Mass: 51239.492 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Compound details | RESIDUES IN AND AROUND THR 96, HIS 129, SER 139, HIS 188, THR 230, LYS 324, AND LEU 358 ARE ALL ...RESIDUES IN AND AROUND THR 96, HIS 129, SER 139, HIS 188, THR 230, LYS 324, AND LEU 358 ARE ALL INVOLVED IN CONTACTS DIRECTLY OR INDIRECTLY | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 50 % | |||||||||||||||
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Crystal grow | *PLUS pH: 6 / Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 294 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 66809 / % possible obs: 94.2 % / Redundancy: 4.04 % / Rmerge(I) obs: 0.0778 |
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Processing
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Refinement | Resolution: 2→8 Å
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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