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- PDB-5xcn: Crystal structure of M120A mutant of O-acetyl-L-serine sulfahydry... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5xcn | ||||||
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Title | Crystal structure of M120A mutant of O-acetyl-L-serine sulfahydrylase from Haemophilus influenzae | ||||||
![]() | Cysteine synthase | ||||||
![]() | TRANSFERASE / Pyridoxal phosphate binding / cysteine synthase activity / L-cysteine desulfhydrase activity / transferase activity / serine acetyl transferase interacting protein | ||||||
Function / homology | ![]() cysteine synthase / cystathionine beta-synthase activity / cysteine synthase activity / L-cysteine desulfhydrase activity / cysteine biosynthetic process from serine / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Abhishek, K. / Kumaran, S. | ||||||
![]() | ![]() Title: Molecular Mechanism of Selective Substrate Engagement and Inhibitor Dis-engagement of Cysteine Synthase. Authors: Kaushik, A. / Rahisuddin, R. / Saini, N. / Singh, R.P. / Kaur, R. / Kaul, S. / Kumaran, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.9 KB | Display | ![]() |
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PDB format | ![]() | 56.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.9 KB | Display | ![]() |
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Full document | ![]() | 426.8 KB | Display | |
Data in XML | ![]() | 15.2 KB | Display | |
Data in CIF | ![]() | 22.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5xcpC ![]() 5xcwC ![]() 7c35C ![]() 7cm8C ![]() 4ho1S C: citing same article ( 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 37144.273 Da / Num. of mol.: 1 / Mutation: M120A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 51907 / DSM 11121 / KW20 / Rd / Gene: cysK, HI_1103 / Plasmid: pET28A / Details (production host): N terminal Histag Production host: ![]() ![]() References: UniProt: P45040, cysteine synthase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37.48 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 100mM HEPES buffer at pH7.5, 1.3M sodium citrate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: May 10, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5 Å / Relative weight: 1 |
Reflection | Resolution: 1.69→28.07 Å / Num. obs: 30261 / % possible obs: 100 % / Redundancy: 4.8 % / Biso Wilson estimate: 23 Å2 / CC1/2: 0.99 / Rmerge(I) obs: 0.05 / Net I/σ(I): 28.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4HO1 Resolution: 1.69→27 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 19.81
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Solvent computation | Shrinkage radii: 0.73 Å / VDW probe radii: 1 Å / Bsol: 47.751 Å2 / ksol: 0.386 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.69→27 Å
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Refine LS restraints |
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LS refinement shell |
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