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Open data
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Basic information
Entry | Database: PDB / ID: 2jad | ||||||
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Title | Yellow fluorescent protein - glutaredoxin fusion protein | ||||||
![]() | YELLOW FLUORESCENT PROTEIN GLUTAREDOXIN FUSION PROTEIN | ||||||
![]() | ELECTRON TRANSPORT / YELLOW FLUORESCENT PROTEIN / REDOX- ACTIVE CENTER / YEAST / GRX1P / TRANSPORT / GLUTAREDOXIN | ||||||
Function / homology | ![]() protein glutathionylation / glutathione peroxidase / glutathione disulfide oxidoreductase activity / glutathione peroxidase activity / glutathione transferase / glutathione transferase activity / bioluminescence / generation of precursor metabolites and energy / cellular response to oxidative stress / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hakansson, K.O. / Winther, J.R. | ||||||
![]() | ![]() Title: Structure of Glutaredoxin Grx1P C30S Mutant from Yeast. Authors: Hakansson, K.O. / Winther, J.R. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2006 Title: Crystallisation of Mutant Forms of Glutaredoxin Grx1P from Yeast Authors: Hakansson, K.O. / Winther, J.R. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.2 KB | Display | ![]() |
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PDB format | ![]() | 58.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449.4 KB | Display | ![]() |
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Full document | ![]() | 456.7 KB | Display | |
Data in XML | ![]() | 16 KB | Display | |
Data in CIF | ![]() | 21.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2jacC ![]() 1h6rS 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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Unit cell |
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Components
#1: Protein | Mass: 40975.215 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Details: THE MUTATED RESIDUE NUMBER 276 CORRESPONDS TO C30S IN GLUTAREDOXIN Source: (gene. exp.) ![]() ![]() ![]() ![]() Production host: ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.6 Å3/Da / Density % sol: 66 % |
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Crystal grow | pH: 10 / Details: 50MM BICARBONATE PH 10 1.5-1.75M MGSO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 30, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.115 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→20 Å / Num. obs: 15714 / % possible obs: 96.7 % / Observed criterion σ(I): -10 / Redundancy: 2.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 5.8 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 2.1 / % possible all: 95.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1H6R Resolution: 2.7→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: RESIDUES 237-241 BUILT AS AAAGG AND RESIDUES 242-245 ABSENT DUE TO DISORDER. THE C-TERMINUS WAS ALSO DISORDERED
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Refinement step | Cycle: LAST / Resolution: 2.7→20 Å
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Refine LS restraints |
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