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Open data
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Basic information
Entry | Database: PDB / ID: 1lxt | ||||||
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Title | STRUCTURE OF PHOSPHOTRANSFERASE PHOSPHOGLUCOMUTASE FROM RABBIT | ||||||
![]() | PHOSPHOGLUCOMUTASE (DEPHOSPHO FORM) | ||||||
![]() | PHOSPHOTRANSFERASE / PHOSPHOGLUCOMUTASE / DEPHOSPHOFORM | ||||||
Function / homology | ![]() phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) / phosphoglucomutase activity / sarcoplasmic reticulum / glucose metabolic process / magnesium ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ray Junior, W.J. / Baranidharan, S. / Liu, Y. | ||||||
![]() | ![]() Title: Structure of rabbit muscle phosphoglucomutase refined at 2.4 A resolution. Authors: Liu, Y. / Ray, W.J. / Baranidharan, S. #1: ![]() Title: Structural Changes at the Metal Ion Binding Site During the Phosphoglucomutase Reaction Authors: Ray Junior, W.J. / Post, C.B. / Liu, Y. / Rhyu, G.I. #2: ![]() Title: The Crystal Structure of Muscle Phosphoglucomutase Refined at 2.7-Angstrom Resolution Authors: Dai, J.B. / Liu, Y. / Ray Junior, W.J. / Konno, M. #3: ![]() Title: The Catalytic Activity of Muscle Phosphoglucomutase in the Crystalline Phase Authors: Ray Junior, W.J. #4: ![]() Title: The Structure of Rabbit Muscle Phosphoglucomutase at Intermediate Resolution Authors: Lin, Z. / Konno, M. / Abad-Zapatero, C. / Wierenga, R. / Murthy, M.R. / Ray Junior, W.J. / Rossmann, M.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 231.7 KB | Display | ![]() |
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PDB format | ![]() | 185.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 451.9 KB | Display | ![]() |
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Full document | ![]() | 496.8 KB | Display | |
Data in XML | ![]() | 48.4 KB | Display | |
Data in CIF | ![]() | 67.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3pmgSC S: Starting model for refinement C: citing same article ( |
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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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 61499.926 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P00949, phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.13 Å3/Da / Density % sol: 61 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: unknown | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Nov 1, 1992 |
Radiation | Monochromator: NI / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.57→30 Å / Num. obs: 45619 / % possible obs: 97 % / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.15 |
Reflection shell | Resolution: 2.7→2.8 Å / % possible all: 60 |
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Processing
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Refinement | Method to determine structure: MODEL REFINEMENT Starting model: PDB ENTRY 3PMG Resolution: 2.7→6 Å / σ(F): 2
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Displacement parameters | Biso mean: 35 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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