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- PDB-2ilu: Crystal structure of lactaldehyde dehydrogenase from E. coli: the... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ilu | ||||||
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Title | Crystal structure of lactaldehyde dehydrogenase from E. coli: the binary complex with NADPH | ||||||
![]() | Aldehyde dehydrogenase A | ||||||
![]() | OXIDOREDUCTASE / NADPH-Lactaldehyde dehydrogenase complex | ||||||
Function / homology | ![]() glycolaldehyde dehydrogenase / glycolaldehyde dehydrogenase (NAD+) activity / lactaldehyde dehydrogenase / succinate-semialdehyde dehydrogenase (NAD+) activity / lactaldehyde dehydrogenase (NAD+) activity / gamma-aminobutyric acid catabolic process / L-fucose catabolic process / rhamnose catabolic process / protein-containing complex / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Di Costanzo, L. / Gomez, G. / Christianson, D.W. | ||||||
![]() | ![]() Title: Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity. Authors: Di Costanzo, L. / Gomez, G.A. / Christianson, D.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 105.2 KB | Display | ![]() |
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PDB format | ![]() | 80.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 846.6 KB | Display | ![]() |
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Full document | ![]() | 858 KB | Display | |
Data in XML | ![]() | 20.7 KB | Display | |
Data in CIF | ![]() | 27.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2hg2SC ![]() 2impC S: Starting model for refinement C: citing same article ( |
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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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Details | The biological assembly is a tetramer generated from the monomer in the asymmetric unit by the operations: -x, -y, z (4); y, x, -z+1/3 (7); -y, -x, -z+1/3 (10) |
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Components
#1: Protein | Mass: 52372.527 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P25553, lactaldehyde dehydrogenase, glycolaldehyde dehydrogenase | ||||
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#2: Chemical | #3: Chemical | ChemComp-NDP / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.09 Å3/Da / Density % sol: 60.17 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 0.1 M Bis-Tris or Tris, 2.0 M ammonium sulfate, pH pH 6.8 - 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 5, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9798 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 16757 / Redundancy: 14.4 % / Rmerge(I) obs: 0.139 / Net I/σ(I): 22.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2HG2 Resolution: 2.7→50 Å
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Refinement step | Cycle: LAST / Resolution: 2.7→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.8 Å / Rfactor Rfree: 0.2945 / Rfactor Rwork: 0.2506 |