+
Open data
-
Basic information
Entry | Database: PDB / ID: 1zcu | ||||||
---|---|---|---|---|---|---|---|
Title | apo form of the 162S mutant of glycogenin | ||||||
![]() | Glycogenin-1 | ||||||
![]() | TRANSFERASE | ||||||
Function / homology | ![]() glycogenin glucosyltransferase / glycogenin glucosyltransferase activity / : / glycogen biosynthetic process / manganese ion binding / protein homodimerization activity / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hurley, T.D. / Stout, S.L. / Miner, E. / Zhou, J. / Roach, P.J. | ||||||
![]() | ![]() Title: Requirements for catalysis in mammalian glycogenin. Authors: Hurley, T.D. / Stout, S. / Miner, E. / Zhou, J. / Roach, P.J. #1: ![]() Title: The structure of the autocatalytic initiator for glycogen biosynthesis, glycogenin Authors: Gibbons, B.J. / Roach, P.J. / Hurley, T.D. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 68.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 49.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.5 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 431 KB | Display | |
Data in XML | ![]() | 12.1 KB | Display | |
Data in CIF | ![]() | 16.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zctC ![]() 1zcvC ![]() 1zcyC ![]() 1zdfC ![]() 1zdgC ![]() 1ll3S S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Components on special symmetry positions |
|
-
Components
#1: Protein | Mass: 39576.195 Da / Num. of mol.: 1 / Mutation: D162S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 47.5 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.4 Details: sodium MES, ammonium sulfate, PEG MME 5000, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 93 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Apr 28, 2004 / Details: osmic confocal |
Radiation | Monochromator: osmic confocal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→25 Å / Num. all: 25865 / Num. obs: 24514 / % possible obs: 94.9 % / Observed criterion σ(F): 0.2 / Observed criterion σ(I): 0.2 / Redundancy: 3.5 % / Biso Wilson estimate: 30.9 Å2 / Rmerge(I) obs: 0.043 / Net I/σ(I): 22.3 |
Reflection shell | Resolution: 2→2.07 Å / Rmerge(I) obs: 0.31 / Mean I/σ(I) obs: 3 / % possible all: 69.2 |
-
Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1LL3 Resolution: 2→25 Å / Isotropic thermal model: restrained / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Bsol: 20.751 Å2 | |||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.553 Å2
| |||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
| |||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→25 Å
| |||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
|