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Yorodumi- PDB-1o0s: Crystal Structure of Ascaris suum Malic Enzyme Complexed with NADH -
+Open data
-Basic information
Entry | Database: PDB / ID: 1o0s | ||||||
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Title | Crystal Structure of Ascaris suum Malic Enzyme Complexed with NADH | ||||||
Components | NAD-dependent malic enzyme | ||||||
Keywords | OXIDOREDUCTASE / Oxidative decarboxylase / Rossmann Fold / Malate dehydrogenase / Ascaris suum | ||||||
Function / homology | Function and homology information malate dehydrogenase (oxaloacetate-decarboxylating) / malate dehydrogenase (decarboxylating) (NAD+) activity / oxaloacetate decarboxylase activity / metabolic process / NAD binding / mitochondrial matrix / metal ion binding Similarity search - Function | ||||||
Biological species | Ascaris suum (pig roundworm) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Rao, G.S. / Coleman, D.E. / Karsten, W.E. / Cook, P.F. / Harris, B.G. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003 Title: Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site. Authors: Rao, G.S. / Coleman, D.E. / Karsten, W.E. / Cook, P.F. / Harris, B.G. #1: Journal: Biochemistry / Year: 2002 Title: Crystal Structure of the Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide at 2.3 A Resolution Authors: Coleman, D.E. / Rao, G.S.J. / Goldsmith, E.J. / Cook, P.F. / Harris, B.G. | ||||||
History |
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Remark 400 | COMPOUND STRUCTURE REVEALS A DIFFERENT ORIENTATION OF THE NICOTINAMIDE RING, COMPARED TO ITS ...COMPOUND STRUCTURE REVEALS A DIFFERENT ORIENTATION OF THE NICOTINAMIDE RING, COMPARED TO ITS POSITION IN THE ENZYME_NAD COMPLEX. STRUCTURE ALSO REVEALS THE BINDING OF TARTRONATE IN AN ALLOSTERIC SITE. | ||||||
Remark 999 | SEQUENCE THE NUMBERING SYSTEM USED FOR THE COORDINATES CORRESPONDS TO THE NUMBERING SYSTEM USED IN ... SEQUENCE THE NUMBERING SYSTEM USED FOR THE COORDINATES CORRESPONDS TO THE NUMBERING SYSTEM USED IN PUBLISHED MUTATIONAL STUDIES, WHERE RESIDUE 1 (LYS) IS THE FIRST RESIDUE PRESENT IN THE FULLY PROCESSED PROTEIN CHAIN. A 12 RESIDUE MITOCHONDRIAL TRANSPORT SEQUENCE IS PRESENT IN THE UNPROCESSED PROTEIN, BUT IS ABSENT FROM PROCESSED PROTEIN AND THE PROTEIN PRESENT IN THE CRYSTALS. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1o0s.cif.gz | 264.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1o0s.ent.gz | 211.9 KB | Display | PDB format |
PDBx/mmJSON format | 1o0s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o0/1o0s ftp://data.pdbj.org/pub/pdb/validation_reports/o0/1o0s | HTTPS FTP |
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-Related structure data
Related structure data | 1llqS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 68556.406 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Ascaris suum (pig roundworm) References: UniProt: P27443, malate dehydrogenase (oxaloacetate-decarboxylating) #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 54.29 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: PEG 4000, sodium acetate, sodium tartronate, NADH, magnesium sulphate, mercaptoethanol, tris, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.3 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.992 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 18, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.992 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. all: 98317 / Num. obs: 98317 / % possible obs: 98.4 % / Observed criterion σ(I): -3 / Redundancy: 6.75 % / Biso Wilson estimate: 30 Å2 / Rmerge(I) obs: 0.093 / Net I/σ(I): 21.6 |
Reflection shell | Resolution: 2→2.09 Å / Redundancy: 2.74 % / Rmerge(I) obs: 0.528 / Mean I/σ(I) obs: 2.77 / Num. unique all: 12159 / % possible all: 98.4 |
Reflection | *PLUS Num. obs: 104791 / % possible obs: 98.7 % / Num. measured all: 693156 / Rmerge(I) obs: 0.056 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1LLQ Resolution: 2→50 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber / Details: Reflections with F<0.0 not used. Bulk solvent correction used throughtout.
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Displacement parameters | Biso mean: 39.7 Å2 | |||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.07 Å
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Software | *PLUS Name: CNS / Version: 1.1 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS % reflection Rfree: 5 % / Rfactor Rfree: 0.272 / Rfactor Rwork: 0.23 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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