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- PDB-1m8p: Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state -
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Open data
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Basic information
Entry | Database: PDB / ID: 1m8p | ||||||
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Title | Crystal Structure of P. chrysogenum ATP Sulfurylase in the T-state | ||||||
![]() | sulfate adenylyltransferase | ||||||
![]() | TRANSFERASE / Rossmann fold / phosphosulfate binding / T-state | ||||||
Function / homology | ![]() sulfur amino acid metabolic process / sulfate assimilation via adenylyl sulfate reduction / sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) / sulfate adenylyltransferase / adenylylsulfate kinase activity / sulfate adenylyltransferase (ATP) activity / hydrogen sulfide biosynthetic process / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | MacRae, I.J. / Segel, I.H. / Fisher, A.J. | ||||||
![]() | ![]() Title: Allosteric Inhibition via R-State Destabilization in ATP Sulfurylase from Penicillium chrysogenum Authors: MacRae, I.J. / Segel, I.H. / Fisher, A.J. | ||||||
History |
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Remark 999 | SEQUENCE AUTHORS state THAT Gly 369 is not an insertion into their sequence and that the original ...SEQUENCE AUTHORS state THAT Gly 369 is not an insertion into their sequence and that the original published sequence was missing this residue. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 351.3 KB | Display | ![]() |
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PDB format | ![]() | 285.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 74.3 KB | Display | |
Data in CIF | ![]() | 101.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1i2dS S: Starting model for refinement |
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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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Details | The second part of the biological assembly is generated by the two fold axis: |
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Components
#1: Protein | Mass: 64062.492 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.23 Å3/Da / Density % sol: 61.93 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG 8000, magnesium chloride, tris(hydroxymethyl)aminomethane, 3'-phosphoadenosine-5'-phosphosulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 67 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: ADSC QUANTUM 4 / Detector: CCD / Date: May 1, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→50 Å / Num. all: 77547 / Num. obs: 77547 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 5.1 % / Biso Wilson estimate: 63.2 Å2 / Rmerge(I) obs: 0.058 / Rsym value: 0.058 |
Reflection shell | Resolution: 2.6→2.7 Å / Rmerge(I) obs: 0.248 / Mean I/σ(I) obs: 3.6 / Num. unique all: 8436 / % possible all: 98.5 |
Reflection | *PLUS Lowest resolution: 50 Å / Num. measured all: 391636 |
Reflection shell | *PLUS % possible obs: 98.5 % / Redundancy: 3.2 % / Num. unique obs: 8436 / Num. measured obs: 26754 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1I2D Resolution: 2.6→29.33 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 186973.94 / Data cutoff high rms absF: 3186973.94 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 42.5433 Å2 / ksol: 0.318152 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 67 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→29.33 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.76 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 30 Å / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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