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- PDB-3iu0: Structural basis for zymogen activation and substrate binding of ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3iu0 | ||||||
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Title | Structural basis for zymogen activation and substrate binding of transglutaminase from Streptomyces mobaraense | ||||||
![]() | Protein-glutamine gamma-glutamyltransferase | ||||||
![]() | TRANSFERASE / MTGase / zymogen / pro-enzyme / cross-linking / Acyltransferase | ||||||
Function / homology | ![]() protein-glutamine gamma-glutamyltransferase / protein-glutamine gamma-glutamyltransferase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Li, T.T. | ||||||
![]() | ![]() Title: Structural basis for zymogen activation and substrate binding of transglutaminase from Streptomyces mobaraense Authors: Yang, M. / Wang, J.M. / Wu, T.K. / Li, T.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.4 KB | Display | ![]() |
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PDB format | ![]() | 62.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 420.3 KB | Display | ![]() |
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Full document | ![]() | 422.9 KB | Display | |
Data in XML | ![]() | 15.3 KB | Display | |
Data in CIF | ![]() | 21.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1iu4S 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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Unit cell |
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Components
#1: Protein | Mass: 43333.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P81453, protein-glutamine gamma-glutamyltransferase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.2 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 30% PEG8000, 50mM NaCl, 1mM EDTA, 1mM beta-mercaptoethanol, 0.01% NaN3, 100mM cacodylic acid, pH5.0 and 2% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 180 K |
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Diffraction source | Source: ![]() |
Radiation | Monochromator: blue-optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 29327 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 8.2 % / Biso Wilson estimate: 27.7 Å2 / Rmerge(I) obs: 0.043 / Net I/σ(I): 39.2 |
Reflection shell | Resolution: 1.9→1.99 Å / Redundancy: 8 % / Rmerge(I) obs: 0.238 / Mean I/σ(I) obs: 8.1 / Num. unique all: 3592 / Rsym value: 0.238 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1IU4 Resolution: 1.9→19.129 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.929 / WRfactor Rfree: 0.244 / WRfactor Rwork: 0.21 / SU B: 3.246 / SU ML: 0.098 / Cross valid method: THROUGHOUT / ESU R: 0.185 / ESU R Free: 0.16 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.615 Å2
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Refine analyze | Luzzati coordinate error obs: 0.278 Å / Luzzati d res low obs: 6 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→19.129 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20
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