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- PDB-1jcm: TRPC STABILITY MUTANT CONTAINING AN ENGINEERED DISULPHIDE BRIDGE ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1jcm | ||||||
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Title | TRPC STABILITY MUTANT CONTAINING AN ENGINEERED DISULPHIDE BRIDGE AND IN COMPLEX WITH A CDRP-RELATED SUBSTRATE | ||||||
![]() | INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE | ||||||
![]() | LYASE / beta-alpha-barrel / disulphide bridge / stability mutant | ||||||
Function / homology | ![]() phosphoribosylanthranilate isomerase / indole-3-glycerol-phosphate synthase / indole-3-glycerol-phosphate synthase activity / phosphoribosylanthranilate isomerase activity / tryptophan biosynthetic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ivens, A. / Mayans, O. / Szadkowski, H. / Wilmanns, M. / Kirschner, K. | ||||||
![]() | ![]() Title: Stabilization of a (betaalpha)8-barrel protein by an engineered disulfide bridge. Authors: Ivens, A. / Mayans, O. / Szadkowski, H. / Jurgens, C. / Wilmanns, M. / Kirschner, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.2 KB | Display | ![]() |
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PDB format | ![]() | 51.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 28916.039 Da / Num. of mol.: 1 Fragment: N-TERMINAL DOMAIN (1-259 AA) OF THE BIFUNCTIONAL ENZYME ANTHRANILATE ISOMERASE, IGPS:PRAI Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: GenBank: 775124, UniProt: P00909*PLUS, indole-3-glycerol-phosphate synthase | ||||
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#2: Chemical | ChemComp-PO4 / #3: Chemical | ChemComp-137 / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.81 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 50 mM potassium phosphate pH 5.0, 1.2 M ammonium sulphate, 5 mM EDTA, pH 5.0, VAPOR DIFFUSION, HANGING DROP at 293K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 8 ℃ / Details: Wilmanns, M., (1990) Protein Eng., 3, 173. / pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.911 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 17306 / Redundancy: 8.8 % / Biso Wilson estimate: 52.7 Å2 / Rsym value: 0.041 / Net I/σ(I): 24.1 |
Reflection shell | Resolution: 2.1→2.15 Å / Redundancy: 2.6 % / Mean I/σ(I) obs: 3.5 / Num. unique all: 935 / Rsym value: 0.25 |
Reflection | *PLUS Lowest resolution: 20 Å / % possible obs: 93.7 % / Rmerge(I) obs: 0.041 |
Reflection shell | *PLUS % possible obs: 78 % / Rmerge(I) obs: 0.25 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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LS refinement shell | Resolution: 2.1→2.2 Å /
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Refinement | *PLUS Lowest resolution: 20 Å / Rfactor obs: 0.241 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
LS refinement shell | *PLUS Rfactor obs: 0.44 |