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- PDB-2ldx: CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ldx | ||||||||||||
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Title | CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4 | ||||||||||||
![]() | APO-LACTATE DEHYDROGENASE | ||||||||||||
![]() | OXIDOREDUCTASE(CHOH(D)-NAD(A)) | ||||||||||||
Function / homology | ![]() lactate biosynthetic process from pyruvate / Pyruvate metabolism / : / flagellated sperm motility / ATP biosynthetic process / L-lactate dehydrogenase / L-lactate dehydrogenase activity / motile cilium / pyruvate metabolic process / cilium ...lactate biosynthetic process from pyruvate / Pyruvate metabolism / : / flagellated sperm motility / ATP biosynthetic process / L-lactate dehydrogenase / L-lactate dehydrogenase activity / motile cilium / pyruvate metabolic process / cilium / carbohydrate metabolic process / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() | ||||||||||||
![]() | Griffith, J.P. / Rossmann, M.G. | ||||||||||||
![]() | ![]() Title: Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4. Authors: Hogrefe, H.H. / Griffith, J.P. / Rossmann, M.G. / Goldberg, E. #1: ![]() Title: The Structure of Mouse Testicular Lactate Dehydrogenase Isoenzyme C4 at 2.9 Angstroms Resolution Authors: Musick, W.D.L. / Rossmann, M.G. #2: ![]() Title: A Low-Resolution Study of Testicular Lactate Dehydrogenase Using the Molecular Replacement Technique Authors: Musick, W.D.L. / Adams, A.D. / Rossmann, M.G. / Wheat, T.E. / Goldberg, E. #3: ![]() Title: A Crystalline Form of Testes-Specific Lactate Dehydrogenase Authors: Adams, A.D. / Adams, M.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 | ![]() | 251.8 KB | Display | ![]() |
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PDB format | ![]() | 197.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.5 KB | Display | ![]() |
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Full document | ![]() | 675.7 KB | Display | |
Data in XML | ![]() | 80.7 KB | Display | |
Data in CIF | ![]() | 104 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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Unit cell |
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Atom site foot note | 1: RESIDUE PRO 138 IS A CIS-PROLINE. | ||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 35866.605 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Water | ChemComp-HOH / | Compound details | THE SECONDARY STRUCTURE SPECIFICAT | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.51 % | |||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.4 / Method: microdialysis / Details: seeding | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.96 Å / Lowest resolution: 10 Å / % possible obs: 0.66 % / Num. measured all: 20475 / Rmerge(I) obs: 0.254 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.96→10 Å / Rfactor obs: 0.256 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.96→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.96 Å / Lowest resolution: 10 Å / Rfactor obs: 0.256 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |