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Yorodumi- PDB-1srx: THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1srx | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 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 / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Soderberg, B.-O. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1975 Title: Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution. Authors: Holmgren, A. / Soderberg, B.O. / Eklund, H. / Branden, C.I. #1: 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1srx.cif.gz | 13.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1srx.ent.gz | 5.7 KB | Display | PDB format |
PDBx/mmJSON format | 1srx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sr/1srx ftp://data.pdbj.org/pub/pdb/validation_reports/sr/1srx | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 11759.448 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: B / References: UniProt: P0AA25 |
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Compound details | THE ACTIVE SITE DISULFIDE BOND IS BETWEEN CYS-32 AND CYS-35 SITE S-S IS THE ACTIVE CENTER DISULFIDE ...THE ACTIVE SITE DISULFIDE BOND IS BETWEEN CYS-32 AND CYS-35 SITE S-S IS THE ACTIVE CENTER DISULFIDE BRIDGED REVERSE TURN. RESIDUES OTHER THAN THOSE GIVEN UNDER SITE BELOW MAY BE INVOLVED IN THE ACTIVITY. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 5.39 Å3/Da / Density % sol: 77.17 % |
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Crystal grow | *PLUS Method: other / Details: Soderberg, B.O., (1974) J. Mol. Biol., 90, 143. |
-Processing
Refinement | Highest resolution: 2.8 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
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