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Yorodumi- PDB-2trx: CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT 1.68 AN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2trx | ||||||
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Title | CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT 1.68 ANGSTROMS RESOLUTION | ||||||
Components | THIOREDOXIN | ||||||
Keywords | ELECTRON TRANSPORT | ||||||
Function / homology | Function and homology information DNA polymerase processivity factor activity / protein-disulfide reductase activity / cell redox homeostasis / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.68 Å | ||||||
Authors | Katti, S.K. / Lemaster, D.M. / Eklund, H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1990 Title: Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. Authors: Katti, S.K. / LeMaster, D.M. / Eklund, H. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1975 Title: Three-Dimensional Structure of Escherichia Coli Thioredoxin-S2 to 2.8 Angstroms Resolution Authors: Holmgren, A. / Soderberg, B.-O. / Eklund, H. / Branden, C.-I. #2: Journal: J.Mol.Biol. / Year: 1974 Title: Structure of Oxidized Thioredoxin to 4.5 Angstroms Resolution Authors: Soderberg, B.-O. / Holmgren, A. / Branden, C.-I. #3: Journal: J.Mol.Biol. / Year: 1970 Title: Crystallization and Preliminary Crystallographic Data for Thioredoxin from Escherichia Coli B Authors: Holmgren, A. / Soderberg, B.-O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2trx.cif.gz | 54.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2trx.ent.gz | 43.9 KB | Display | PDB format |
PDBx/mmJSON format | 2trx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2trx_validation.pdf.gz | 391 KB | Display | wwPDB validaton report |
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Full document | 2trx_full_validation.pdf.gz | 395.1 KB | Display | |
Data in XML | 2trx_validation.xml.gz | 6.7 KB | Display | |
Data in CIF | 2trx_validation.cif.gz | 10.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tr/2trx ftp://data.pdbj.org/pub/pdb/validation_reports/tr/2trx | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO A 76 AND PRO B 76 ARE CIS PROLINES. 2: RESIDUES HIS A 6, LEU A 7, ILE A 23, ASP A 47, GLU A 48, LEU A 58, LEU A 80, HIS B 6, ASP B 47, LEU B 58, AND LEU B 80 HAVE BEEN MODELED AS TWO CONFORMERS. 3: RESIDUES 11 - 21 IN CHAIN B ARE DISORDERED. |
-Components
#1: Protein | Mass: 11687.388 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0AA25 #2: Chemical | #3: Chemical | ChemComp-MPD / ( #4: 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: 54.58 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 3.8 / Method: microdialysis / Details: equilibrium dialysis | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.68 Å / Lowest resolution: 2.5 Å / Num. obs: 27483 / Rmerge F obs: 0.063 |
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-Processing
Software | Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.68→8 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 1.68→8 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 26415 / Rfactor obs: 0.165 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |