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- PDB-1gpd: STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gpd | |||||||||
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Title | STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | |||||||||
![]() | D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | |||||||||
![]() | OXIDOREDUCTASE / OXIDO-REDUCTASE(ALDEHYDE/DONR / NAD/ACCPT) / OXIDO-REDUCTASE(ALDEHYDE-DONR / NAD-ACCPT) COMPLEX | |||||||||
Function / homology | ![]() glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / glycolytic process / glucose metabolic process / NAD binding / NADP binding / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Moras, D. / Olsen, K.W. / Sabesan, M.N. / Buehner, M. / Ford, G.C. / Rossmann, M.G. | |||||||||
![]() | ![]() Title: Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase. Authors: Moras, D. / Olsen, K.W. / Sabesan, M.N. / Buehner, M. / Ford, G.C. / Rossmann, M.G. #1: ![]() Title: Anion Binding Sites in the Active Center of D-Glyceraldehyde-3-Phosphate Dehydrogenase Authors: Olsen, K.W. / Garavito, R.M. / Sabesan, M.N. / Rossmann, M.G. #2: ![]() Title: Studies on Coenzyme Binding to Glyceraldehyde-3-Phosphate Dehydrogenase Authors: Olsen, K.W. / Garavito, R.M. / Sabesan, M.N. / Rossmann, M.G. #3: ![]() Year: 1975 Title: A Comparison of the Binding and Function of Nad with Respect to Lactate Dehydrogenase and Glyceraldehyde-3-Phosphate Dehydrogenase Authors: Rossmann, M.G. #4: ![]() Title: Sequence Variability and Structure of D-Glyceraldehyde-3-Phosphate Dehydrogenase Authors: Olsen, K.W. / Moras, D. / Rossmann, M.G. / Harris, J.I. #5: ![]() Title: Three-Dimensional Structure of D-Glyceraldehyde-3-Phosphate Dehydrogenase Authors: Buehner, M. / Ford, G.C. / Moras, D. / Olsen, K.W. / Rossmann, M.G. #6: ![]() Title: Structure Determination of Crystalline Lobster D-Glyceraldehyde-3-Phosphate Dehydrogenase Authors: Buehner, M. / Ford, G.C. / Moras, D. / Olsen, K.W. / Rossmann, M.G. #7: ![]() Title: D-Glyceraldehyde-3-Phosphate Dehydrogenase,Three Dimensional Structure and Evolutionary Significance Authors: Buehner, M. / Ford, G.C. / Moras, D. / Olsen, K.W. / Rossmann, M.G. #8: ![]() Title: An Application of the Molecular Replacement Technique in Direct Space to a Known Protein Structure Authors: Argos, P. / Ford, G.C. / Rossmann, M.G. | |||||||||
History |
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Remark 700 | SHEET THE SHEET SUBSTRUCTURE OF THE CATALYTIC DOMAIN IS BIFURCATED. TO REPRESENT THIS FEATURE ...SHEET THE SHEET SUBSTRUCTURE OF THE CATALYTIC DOMAIN IS BIFURCATED. TO REPRESENT THIS FEATURE REDUNDANT SHEETS ARE DEFINED FOR EACH OF THE TWO SUBUNITS. STRANDS 1-7 OF SHEETS GC1 AND RC1 ARE IDENTICAL TO STRANDS 1-7 OF SHEETS GC2 AND RC2. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 129.2 KB | Display | ![]() |
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PDB format | ![]() | 92.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 551.8 KB | Display | ![]() |
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Full document | ![]() | 772.1 KB | Display | |
Data in XML | ![]() | 46.1 KB | Display | |
Data in CIF | ![]() | 61.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 35783.949 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P00357, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) #2: Chemical | #3: Chemical | ChemComp-PO4 / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.84 Å3/Da / Density % sol: 78.95 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.5 / Method: unknownDetails: (batch), took Watoson & Banaszak from Buehner et al., from original paper. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.9 Å / Num. obs: 13090 / Num. measured all: 33302 |
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Processing
Refinement | Highest resolution: 2.9 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.9 Å
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Refinement | *PLUS Highest resolution: 2.9 Å | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |