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Open data
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Basic information
Entry | Database: PDB / ID: 1geu | ||||||
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Title | ANATOMY OF AN ENGINEERED NAD-BINDING SITE | ||||||
![]() | GLUTATHIONE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE(FLAVOENZYME) | ||||||
Function / homology | ![]() glutathione-disulfide reductase / glutathione-disulfide reductase (NADPH) activity / FAD binding / glutathione metabolic process / cell redox homeostasis / NADP binding / flavin adenine dinucleotide binding / cellular response to oxidative stress / membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Mittl, P.R.E. / Schulz, G.E. | ||||||
![]() | ![]() Title: Anatomy of an engineered NAD-binding site. Authors: Mittl, P.R. / Berry, A. / Scrutton, N.S. / Perham, R.N. / Schulz, G.E. #1: ![]() Title: The Structure of Glutathione Reductase from Escherichia Coli at 1.86 Angstroms Resolution: Comparison with the Enzyme from Human Erythrocytes Authors: Mittl, P.R.E. / Schulz, G.E. #2: ![]() Title: Structural Differences between Wild-Type Nad-Dependent Glutathione Reductase from Escherichia Coli and a Redesigned Nad-Dependent Mutant Authors: Mittl, P.R.E. / Berry, A. / Scrutton, N.S. / Perham, R.N. / Schulz, G.E. #3: ![]() Title: Redesign of the Cofactor Specificity of a Dehydrogenase by Protein Engineering Authors: Scrutton, N.S. / Berry, A. / Perham, R.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 193.9 KB | Display | ![]() |
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PDB format | ![]() | 152.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 39 KB | Display | |
Data in CIF | ![]() | 55.3 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: CIS PROLINE - PRO A 223 / 2: CIS PROLINE - PRO A 347 / 3: CIS PROLINE - PRO A 440 / 4: CIS PROLINE - PRO B 223 / 5: CIS PROLINE - PRO B 347 / 6: CIS PROLINE - PRO B 440 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.996165, 0.002006, -0.087477), Vector: Details | THERE IS A WHOLE DIMER IN THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT. THE SUBUNITS HAVE BEEN ASSIGNED CHAIN IDENTIFIERS A AND B. THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO CHAIN *B*. | |
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Components
#1: Protein | Mass: 48739.129 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Nonpolymer details | ONE NAD IS BOUND PER SUBUNIT. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.48 % |
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Crystal grow | *PLUS Method: unknown |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.2 Å / % possible obs: 82.2 % / Rmerge(I) obs: 0.087 |
Reflection shell | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 2.28 Å / % possible obs: 65 % |
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Processing
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Refinement | Resolution: 2.2→7 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.2→7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 42272 / Rfactor all: 0.169 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3 |