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Open data
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Basic information
Entry | Database: PDB / ID: 2ljr | ||||||
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Title | GLUTATHIONE TRANSFERASE APO-FORM FROM HUMAN | ||||||
![]() | GLUTATHIONE S-TRANSFERASE![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Rossjohn, J. / Mckinstry, W.J. / Oakley, A.J. / Verger, D. / Flanagan, J. / Chelvanayagam, G. / Tan, K.L. / Board, P.G. / Parker, M.W. | ||||||
![]() | ![]() Title: Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Authors: Rossjohn, J. / McKinstry, W.J. / Oakley, A.J. / Verger, D. / Flanagan, J. / Chelvanayagam, G. / Tan, K.L. / Board, P.G. / Parker, M.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 96.3 KB | Display | ![]() |
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PDB format | ![]() | 76.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.197043, 0.980821, -0.010087), Vector ![]() |
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Components
#1: Protein | ![]() Mass: 27537.957 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: APO FORM / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() References: UniProt: P30712, UniProt: P0CG30*PLUS, ![]() #2: Water | ChemComp-HOH / | ![]() Nonpolymer details | TWO WATER MOLECULES HAVE BEEN MODELLED IN THE ACTIVE SITE: ONE PER MONOMER. IT IS BELIEVED, FROM ...TWO WATER MOLECULES HAVE BEEN MODELLED IN THE ACTIVE SITE: ONE PER MONOMER. IT IS BELIEVED, FROM THE STRONG FEATURES IN THE FO - FC MAPS, THAT THESE "WATER" MOLECULES ACTUALLY REPRESENT A SULFATE OR PHOSPHATE ANION. THE LOW RESOLUTION | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.48 % | |||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 277 or 295 K / pH: 7 / Method: vapor diffusion, hanging dropDetails: drop solution was mixed with an equal volume of reservoir solution | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: FILM / Date: Dec 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3.2→15 Å / Num. obs: 9362 / % possible obs: 89.2 % / Redundancy: 1.9 % / Rsym value: 0.109 / Net I/σ(I): 7.9 |
Reflection shell | Resolution: 3.2→3.3 Å / Mean I/σ(I) obs: 2 / % possible all: 87.2 |
Reflection | *PLUS Num. measured all: 17711 / Rmerge(I) obs: 0.109 |
Reflection shell | *PLUS % possible obs: 87.2 % |
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Processing
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Refinement | Resolution: 3.2→15 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 3.2→15 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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