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- PDB-5xcp: Crystal structure of M92A mutant of O-acetyl-L-serine sulfhydryla... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5xcp | ||||||
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Title | Crystal structure of M92A mutant of O-acetyl-L-serine sulfhydrylase from Haemophilus influenzae | ||||||
![]() | Cysteine synthase | ||||||
![]() | TRANSFERASE / pyridoxal phosphate binding / cysteine synthase activity / O-acetylserine (thiol)-lyase / Interacts with Serine acetyl transferase | ||||||
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 | ![]() | 74.7 KB | Display | ![]() |
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PDB format | ![]() | 51.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438.6 KB | Display | ![]() |
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Full document | ![]() | 441.4 KB | Display | |
Data in XML | ![]() | 13.3 KB | Display | |
Data in CIF | ![]() | 17.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5xcnC ![]() 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: M92A 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: 1.94 Å3/Da / Density % sol: 36.59 % / Description: triangle shaped |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.4 / Details: 100mM Hepes buffer pH7.4, 1.4M sodium citrate / PH range: 7.4-7.6 |
-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: Jul 20, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.514 Å / Relative weight: 1 |
Reflection twin | Operator: -k,-h,-l / Fraction: 0.491 |
Reflection | Resolution: 2→19.8 Å / Num. obs: 18182 / % possible obs: 97 % / Redundancy: 7.9 % / Biso Wilson estimate: 16 Å2 / CC1/2: 0.98 / Rmerge(I) obs: 0.048 / Net I/av σ(I): 9.8 / Net I/σ(I): 34 |
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 7.4 % / Rmerge(I) obs: 0.084 / Mean I/σ(I) obs: 8.7 / Num. unique obs: 2308 / % possible all: 85.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4HO1 Resolution: 2.043→19 Å / Cross valid method: FREE R-VALUE / σ(F): 2.04 / Phase error: 16.61
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Solvent computation | Shrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Bsol: 33.994 Å2 / ksol: 0.384 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.043→19 Å
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Refine LS restraints |
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LS refinement shell |
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