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- PDB-8ldh: REFINED CRYSTAL STRUCTURE OF DOGFISH M4 APO-LACTATE DEHYDROGENASE -
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Open data
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Basic information
Entry | Database: PDB / ID: 8ldh | ||||||
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Title | REFINED CRYSTAL STRUCTURE OF DOGFISH M4 APO-LACTATE DEHYDROGENASE | ||||||
![]() | M4 APO-LACTATE DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
Function / homology | ![]() L-lactate dehydrogenase / lactate metabolic process / L-lactate dehydrogenase activity / pyruvate metabolic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Abad-Zapatero, C. / Rossmann, M.G. | ||||||
![]() | ![]() Title: Refined crystal structure of dogfish M4 apo-lactate dehydrogenase. Authors: Abad-Zapatero, C. / Griffith, J.P. / Sussman, J.L. / Rossmann, M.G. #1: ![]() Title: A Comparison of the Structures of Apo Dogfish M4 Lactate Dehydrogenase and its Ternary Complexes Authors: White, J.L. / Hackert, M.L. / Buehner, M. / Adams, M.J. / Ford, G.C. / Lentzjunior, P.J. / Smiley, I.E. / Steindel, S.J. / Rossmann, M.G. #2: ![]() Title: Structural Adaptations of Lactate Dehydrogenase Isozymes Authors: Eventoff, W. / Rossmann, M.G. / Taylor, S.S. / Torff, H.-J. / Meyer, H. / Keil, W. / Kiltz, H.-H. #3: ![]() Title: A 5 Angstroms X-Ray Diffraction Study of Coenzyme-Deficient Lactate Dehydrogenase,Nad-Pyruvate Ternary Complex Authors: White, J. / Rossmann, M.G. / Ford, G.C. #4: ![]() Title: A Structural Comparison of Porcine B4 and Dogfish A4 Isozymes of Lactate Dehydrogenase Authors: Eventoff, W. / Hackert, M.L. / Steindel, S.J. / Rossmann, M.G. #5: ![]() Title: Lactate Dehydrogenase Authors: Holbrook, J.J. / Liljas, A. / Steindel, S.J. / Rossmann, M.G. #6: ![]() Title: X-Ray Studies of Protein Interactions Authors: Liljas, A. / Rossmann, M.G. #7: ![]() Title: Chemical and Biological Evolution of a Nucleotide Binding Protein Authors: Rossmann, M.G. / Moras, D. / Olsen, K.W. #8: ![]() Title: Recognition of Structural Domains in Globular Proteins Authors: Rossmann, M.G. / Liljas, A. #9: ![]() Title: Atomic Co-Ordinates for Dogfish M4 Apo-Lactate Dehydrogenase Authors: Adams, M.J. / Ford, G.C. / Liljas, A. / Rossmann, M.G. #10: ![]() Title: Structure-Function Relationships in Lactate Dehydrogenase Authors: Adams, M.J. / Buehner, M. / Chandrasekhar, K. / Ford, G.C. / Hackert, M.L. / Liljas, A. / Rossmann, M.G. / Smiley, I.E. / Allison, W.S. / Everse, J. / Kaplan, N.O. / Taylor, S.S. #11: ![]() Title: Amino-Acid Sequence of Dogfish M4 Lactate Dehydrogenase Authors: Taylor, S.S. / Oxley, S.S. / Allison, W.S. / Kaplan, N.O. #12: ![]() Title: Molecular Symmetry Axes and Subunit Interfaces in Certain Dehydrogenases Authors: Rossmann, M.G. / Adams, M.J. / Buehner, M. / Ford, G.C. / Hackert, M.L. / Liljas, A. / Rao, S.T. / Banaszak, L.J. / Hill, E. / Tsernoglou, D. / Webb, L. #13: ![]() Title: Functional Anion Binding Sites in Dogfish M4 Lactate Dehydrogenase Authors: Adams, M.J. / Liljas, A. / Rossmann, M.G. #14: ![]() Title: Binding of Oxamate to the Apoenzyme of Dogfish M4 Lactate Dehydrogenase Authors: Mcphersonjunior, A. #15: ![]() Title: Conformation of Coenzyme Fragments When Bound to Lactate Dehydrogenase Authors: Chandrasekhar, K. / Mcphersonjunior, A. / Adams, M.J. / Rossmann, M.G. #16: ![]() Title: The 5 Angstroms Resolution Structure of an Abortive Ternary Complex of Lactate Dehydrogenase and its Comparison with the Apo-Enzyme Authors: Smiley, I.E. / Koekoek, R. / Adams, M.J. / Rossmann, M.G. #17: ![]() Title: Structure of Lactate Dehydrogenase at 2.8 Angstroms Resolution Authors: Adams, M.J. / Ford, G.C. / Koekoek, R. / Lentzjunior, P.J. / Mcphersonjunior, A. / Rossmann, M.G. / Smiley, I.E. / Schevitz, R.W. / Wonacott, A.J. #18: ![]() Title: Low Resolution Study of Crystalline L-Lactate Dehydrogenase Authors: Adams, M.J. / Haas, D.J. / Jeffery, B.A. / Mcphersonjunior, A. / Mermall, H.L. / Rossmann, M.G. / Schevitz, R.W. / Wonacott, A.J. #19: ![]() Title: The Crystal Structure of Lactic Dehydrogenase Authors: Rossmann, M.G. / Jeffery, B.A. / Main, P. / Warren, S. | ||||||
History |
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Remark 700 | SHEET STRAND 2 OF SHEET S2 IS BIFURCATED. THIS IS REPRESENTED BY TWO SHEETS, S2A AND S2B BELOW, ...SHEET STRAND 2 OF SHEET S2 IS BIFURCATED. THIS IS REPRESENTED BY TWO SHEETS, S2A AND S2B BELOW, WHERE THE FIRST STRAND OF IS S2A IS IDENTICAL TO THE FIRST STRAND OF S2B. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 82.7 KB | Display | ![]() |
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PDB format | ![]() | 62.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 392.9 KB | Display | ![]() |
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Full document | ![]() | 436.1 KB | Display | |
Data in XML | ![]() | 15.7 KB | Display | |
Data in CIF | ![]() | 22.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Atom site foot note | 1: RESIDUE PRO 139 IS A CIS PROLINE. | ||||||||
Details | NON-CRYSTALLOGRAPHIC SYMMETRY ELEMENTS CORRESPONDING TO THE THREE ORTHOGONAL MOLECULAR SYMMETRY AXES ARE PRESENTED ON THE MTRIX RECORDS BELOW. |
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Components
#1: Protein | Mass: 36353.297 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | THE RESIDUES IN THIS ENTRY ARE NUMBERED SEQUENTIALLY FROM 0 - 329. SEE THE PAPER CITED AS REFERENCE ...THE RESIDUES IN THIS ENTRY ARE NUMBERED SEQUENTIAL | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 57.26 % |
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Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: referred to 'Pesca, A. J.', (1967) J.Biol.Chem., 242, 2151-2167 |
Components of the solutions | *PLUS Conc.: 30 %sat / Common name: ammonium sulfate |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.191 / Highest resolution: 2.8 Å Details: SPACE GROUP F 4 2 2 IS A NON-STANDARD REPRESENTATION OF THE GROUP I 4 2 2. IN THIS CASE THE AXES OF THE UNIT CELL ARE CONSIDERED TO BE LEFT-HANDED. USING CONVENTIONAL NOTATION THE EQUI- ...Details: SPACE GROUP F 4 2 2 IS A NON-STANDARD REPRESENTATION OF THE GROUP I 4 2 2. IN THIS CASE THE AXES OF THE UNIT CELL ARE CONSIDERED TO BE LEFT-HANDED. USING CONVENTIONAL NOTATION THE EQUI-POINTS OF THE F 4 2 2 CELL MAY BE EXPRESSED AS- ( 0,0,0 0,1/2,1/2 1/2,0,1/2 1/2,1/2,0 ) + X, Y, Z -X,-Y, Z -X, Y,-Z X,-Y,-Z Y, X,-Z -Y,-X,-Z -Y, X, Z Y,-X, Z . | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.8 Å / Rfactor obs: 0.191 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |