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- PDB-1gdh: CRYSTAL STRUCTURE OF A NAD-DEPENDENT D-GLYCERATE DEHYDROGENASE AT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gdh | ||||||
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Title | CRYSTAL STRUCTURE OF A NAD-DEPENDENT D-GLYCERATE DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION | ||||||
![]() | D-GLYCERATE DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE(CHOH (D)-NAD(P)+ (A)) | ||||||
Function / homology | ![]() glycerate dehydrogenase / hydroxypyruvate reductase (NADH) activity / NAD binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Goldberg, J.D. / Yoshida, T. / Brick, P. | ||||||
![]() | ![]() Title: Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution. Authors: Goldberg, J.D. / Yoshida, T. / Brick, P. #1: ![]() Title: Crystallization and Preliminary Diffraction Studies of Hydroxypyruvate Reductase (D-Glycerate Dehydrogenase) from Hyphomicrobium Methylovorum Authors: Goldberg, J.D. / Brick, P. / Yoshida, T. / Mitsunaga, T. / Oshiro, T. / Shimao, M. / Izumi, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 133 KB | Display | ![]() |
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PDB format | ![]() | 105 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 434.6 KB | Display | ![]() |
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Full document | ![]() | 449.1 KB | Display | |
Data in XML | ![]() | 27.3 KB | Display | |
Data in CIF | ![]() | 38 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: CIS PROLINE - PRO A 270 / 2: CIS PROLINE - PRO B 270 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.35079, -0.49109, 0.79736), Vector: |
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Components
#1: Protein | Mass: 34934.406 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.91 Å3/Da / Density % sol: 57.8 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7 / Method: vapor diffusion, hanging drop / Details: Goldberg, J.D., (1992) J.Mol.Biol., 225, 909. | ||||||||||||||||||||||||||||||
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: 2.4 Å / Num. obs: 24903 / % possible obs: 80.8 % / Num. measured all: 41961 / Rmerge(I) obs: 0.048 |
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Processing
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Refinement | Rfactor Rwork: 0.189 / Rfactor obs: 0.189 / Highest resolution: 2.4 Å Details: ONLY PARTIAL DNA SEQUENCE INFORMATION IS AVAILABLE. THE DNA SEQUENCE CORRESPONDING TO THE 130 N-TERMINAL RESIDUES IS KNOWN. FOR THE REMAINDER OF THE POLYPEPTIDE, SIDE-CHAIN IDENTITIES HAVE ...Details: ONLY PARTIAL DNA SEQUENCE INFORMATION IS AVAILABLE. THE DNA SEQUENCE CORRESPONDING TO THE 130 N-TERMINAL RESIDUES IS KNOWN. FOR THE REMAINDER OF THE POLYPEPTIDE, SIDE-CHAIN IDENTITIES HAVE BEEN INTERPRETED DIRECTLY FROM ELECTRON DENSITY MAPS. THE POSSIBILITY OF THERE BEING ADDITIONAL RESIDUES AT THE C-TERMINUS IS NOT DISCOUNTED. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 10 Å / Num. reflection obs: 24553 / Rfactor obs: 0.194 / Rfactor Rwork: 0.194 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.57 |