+Open data
-Basic information
Entry | Database: PDB / ID: 1ges | ||||||
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Title | ANATOMY OF AN ENGINEERED NAD-BINDING SITE | ||||||
Components | GLUTATHIONE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE(FLAVOENZYME) | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.74 Å | ||||||
Authors | Mittl, P.R.E. / Schulz, G.E. | ||||||
Citation | Journal: Protein Sci. / Year: 1994 Title: Anatomy of an engineered NAD-binding site. Authors: Mittl, P.R. / Berry, A. / Scrutton, N.S. / Perham, R.N. / Schulz, G.E. #1: Journal: Protein Sci. / Year: 1994 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: Journal: J.Mol.Biol. / Year: 1993 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: Journal: Nature / Year: 1990 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ges.cif.gz | 191.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ges.ent.gz | 158.1 KB | Display | PDB format |
PDBx/mmJSON format | 1ges.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ges_validation.pdf.gz | 895.6 KB | Display | wwPDB validaton report |
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Full document | 1ges_full_validation.pdf.gz | 907.6 KB | Display | |
Data in XML | 1ges_validation.xml.gz | 39.2 KB | Display | |
Data in CIF | 1ges_validation.cif.gz | 57.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ge/1ges ftp://data.pdbj.org/pub/pdb/validation_reports/ge/1ges | HTTPS FTP |
-Related structure data
-Links
-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: (-0.996127, 0.010365, -0.087312), Vector: Details | THERE IS A WHOLE DIMER IN THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT, THE SUBUNITS ARE MARKED BY DIFFERENT SEGMENT IDS, NAMELY CHAINS A AND B. THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO CHAIN *B*. | |
-Components
#1: Protein | Mass: 48739.129 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P06715, EC: 1.6.4.2 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.62 % |
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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: 1.74 Å / % possible obs: 94 % / Rmerge(I) obs: 0.068 |
Reflection shell | *PLUS Highest resolution: 1.74 Å / Lowest resolution: 1.78 Å / % possible obs: 93 % |
-Processing
Software |
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Refinement | Resolution: 1.74→7 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.74→7 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 100974 / Rfactor obs: 0.168 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.69 |