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Open data
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Basic information
Entry | Database: PDB / ID: 1l9x | ||||||
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Title | Structure of gamma-Glutamyl Hydrolase | ||||||
![]() | gamma-glutamyl hydrolase![]() | ||||||
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Function / homology | ![]() folate gamma-glutamyl hydrolase / tetrahydrofolylpolyglutamate metabolic process / gamma-glutamyl-peptidase activity / neutrophil degranulation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Li, H. / Ryan, T.J. / Chave, K.J. / Van Roey, P. | ||||||
![]() | ![]() Title: Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate. Authors: Li, H. / Ryan, T.J. / Chave, K.J. / Van Roey, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 256.5 KB | Display | ![]() |
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PDB format | ![]() | 213.5 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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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | ![]() Mass: 35988.961 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() References: UniProt: Q92820, folate gamma-glutamyl hydrolase #2: Chemical | ChemComp-BME / ![]() #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.24 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: PEG4000, ammonium acetate, sodium chloride, sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 288.K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: BRANDEIS - B4 / Detector: CCD / Date: Jun 3, 2001 | |||||||||||||||
Radiation | Monochromator: GRAPHITE / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.6→25 Å / Num. all: 161629 / Num. obs: 161520 / % possible obs: 82.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.1 % / Biso Wilson estimate: 21.6 Å2 / Rmerge(I) obs: 0.045 / Rsym value: 0.045 / Net I/σ(I): 53 | |||||||||||||||
Reflection shell | Resolution: 1.6→1.66 Å / Rmerge(I) obs: 0.211 / Mean I/σ(I) obs: 4.4 / Num. unique all: 6118 / Rsym value: 0.211 / % possible all: 31.5 | |||||||||||||||
Reflection | *PLUS Redundancy: 6.3 % / Rmerge(I) obs: 0.045 | |||||||||||||||
Reflection shell | *PLUS % possible obs: 31.5 % / Rmerge(I) obs: 0.211 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Displacement parameters | Biso mean: 24.6 Å2 | |||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.17 Å / Luzzati sigma a obs: 0.2 Å | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→25 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 100 Å / Rfactor obs: 0.182 / Rfactor Rfree![]() ![]() | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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