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Yorodumi- PDB-2tir: CRYSTAL STRUCTURE ANALYSIS OF A MUTANT ESCHERICHIA COLI THIOREDOX... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2tir | ||||||
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Title | CRYSTAL STRUCTURE ANALYSIS OF A MUTANT ESCHERICHIA COLI THIOREDOXIN IN WHICH LYSINE 36 IS REPLACED BY GLUTAMIC ACID | ||||||
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 Å | ||||||
Authors | Nikkola, M. / Gleason, F.K. / Fuchs, J.A. / Eklund, H. | ||||||
Citation | Journal: Biochemistry / Year: 1993 Title: Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid. Authors: Nikkola, M. / Gleason, F.K. / Fuchs, J.A. / Eklund, H. #1: Journal: J.Mol.Biol. / Year: 1990 Title: The Refined Structure of Coli Thioredoxin Authors: Katti, S.K. / Lemaster, D.M. / Eklund, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2tir.cif.gz | 29.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2tir.ent.gz | 22.6 KB | Display | PDB format |
PDBx/mmJSON format | 2tir.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ti/2tir ftp://data.pdbj.org/pub/pdb/validation_reports/ti/2tir | 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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Atom site foot note | 1: CIS PROLINE - PRO 76 2: THE BINDING OF THE CUPRIC ION IS PROBLEMATIC. CLEARLY THE RESIDUES INDICATED DO PARTICIPATE IN THE BINDING. THIS PART OF THE STRUCTURE IS BEING IMPROVED. (CU 109) |
-Components
#1: Protein | Mass: 11687.321 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0AA25 |
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#2: Chemical | ChemComp-CU / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.64 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 4.8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 7477 / Num. measured all: 31697 / Rmerge(I) obs: 0.087 |
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-Processing
Software |
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Refinement | Rfactor Rwork: 0.199 / Rfactor obs: 0.199 / Highest resolution: 2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 7 Å / Rfactor obs: 0.199 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.95 |