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- PDB-2q3c: 2.1 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylas... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2q3c | ||||||
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Title | 2.1 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (OASS) Holoenzyme From MYCOBACTERIUM TUBERCULOSIS in Complex with the Inhibitory Peptide DFSI | ||||||
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![]() | TRANSFERASE / Mycobacterium tuberculosis / Pyridoxal-5'-phosphate / sulphur metabolism / cysteine biosynthesis / SAT / peptide-inhibitor | ||||||
Function / homology | ![]() Cysteine synthesis from O-acetylserine / cysteine synthase / cysteine synthase activity / L-cysteine desulfhydrase activity / cysteine biosynthetic process / cysteine biosynthetic process from serine / pyridoxal phosphate binding / extracellular region / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Schneider, G. / Schnell, R. | ||||||
![]() | ![]() Title: Structural Insights into Catalysis and Inhibition of O-Acetylserine Sulfhydrylase from Mycobacterium tuberculosis: CRYSTAL STRUCTURES OF THE ENZYME {alpha}-AMINOACRYLATE INTERMEDIATE AND AN ...Title: Structural Insights into Catalysis and Inhibition of O-Acetylserine Sulfhydrylase from Mycobacterium tuberculosis: CRYSTAL STRUCTURES OF THE ENZYME {alpha}-AMINOACRYLATE INTERMEDIATE AND AN ENZYME-INHIBITOR COMPLEX. Authors: Schnell, R. / Oehlmann, W. / Singh, M. / Schneider, G. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 76.4 KB | Display | ![]() |
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PDB format | ![]() | 54.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2q3bSC ![]() 2q3dC S: Starting model for refinement C: citing same article ( |
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Similar 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 | The OASS forms a dimer, the second part of the biological assembly is generated by the two fold axis: -y, x, -z. |
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Components
#1: Protein | Mass: 33296.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A534, UniProt: P9WP55*PLUS, cysteine synthase |
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#2: Protein/peptide | Mass: 480.512 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() |
#3: Chemical | ChemComp-MPD / ( |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.61 Å3/Da / Density % sol: 65.96 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 0.1 M HEPES, 80% MPD, 4 mM DFSI-peptide, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Mar 3, 2007 |
Radiation | Monochromator: Diamond(111), Ge(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→59.66 Å / Num. all: 26571 / Num. obs: 26571 / % possible obs: 93.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Biso Wilson estimate: 31 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 11.5 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 5 % / Rmerge(I) obs: 0.352 / Mean I/σ(I) obs: 3.3 / Num. unique all: 3941 / % possible all: 96.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 2Q3B, Holoenzyme Resolution: 2.1→51.23 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.944 / SU B: 4.219 / SU ML: 0.108 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.165 / ESU R Free: 0.142 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.734 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→51.23 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.155 Å / Total num. of bins used: 20
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