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Open data
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Basic information
Entry | Database: PDB / ID: 7qc7 | ||||||
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Title | HisF-C9A-D11E-V33A_L50H_I52H mutant (apo) from T. maritima | ||||||
![]() | Imidazole glycerol phosphate synthase subunit HisF | ||||||
![]() | METAL BINDING PROTEIN / BETA BARREL / ARTIFICIAL METALLOENZYME / PROTEIN DESIGN / OXIDOREDUCTASE | ||||||
Function / homology | ![]() imidazole glycerol-phosphate synthase / imidazoleglycerol-phosphate synthase activity / L-histidine biosynthetic process / lyase activity / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Beaumet, M. / Dose, A. / Braeuer, A. / Mahy, J. / Ghattas, W. / Groll, M. / Hess, C. | ||||||
Funding support | European Union, 1items
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![]() | ![]() Title: An artificial metalloprotein with metal-adaptive coordination sites and Ni-dependent quercetinase activity. Authors: Beaumet, M. / Dose, A. / Brauer, A. / Mahy, J.P. / Ghattas, W. / Groll, M. / Hess, C.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 125.7 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.4 KB | Display | ![]() |
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Full document | ![]() | 426.1 KB | Display | |
Data in XML | ![]() | 14.7 KB | Display | |
Data in CIF | ![]() | 22.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7qc3SC ![]() 7qc6C ![]() 7qc8C ![]() 7qc9C S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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 on special symmetry positions |
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Components
#1: Protein | Mass: 27713.639 Da / Num. of mol.: 1 / Mutation: C9A, D11E, V33A, L50H, I52H Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8 Gene: hisF, TM_1036 / Production host: ![]() ![]() References: UniProt: Q9X0C6, imidazole glycerol-phosphate synthase |
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#2: Chemical | ChemComp-MES / |
#3: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.72 Å3/Da / Density % sol: 66.94 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 8.3 / Details: 100 mM TRIS, 23% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 15, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→30 Å / Num. obs: 55939 / % possible obs: 99.5 % / Redundancy: 5.5 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 16.6 |
Reflection shell | Resolution: 1.6→1.7 Å / Rmerge(I) obs: 0.541 / Num. unique obs: 9169 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 7QC3 Resolution: 1.6→15 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.973 / SU B: 2.3 / SU ML: 0.035 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.06 / ESU R Free: 0.054 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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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: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 92.9 Å2 / Biso mean: 27.237 Å2 / Biso min: 13.56 Å2
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Refinement step | Cycle: final / Resolution: 1.6→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.6→1.641 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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