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- PDB-2tir: CRYSTAL STRUCTURE ANALYSIS OF A MUTANT ESCHERICHIA COLI THIOREDOX... -
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Open data
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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 | ||||||
![]() | THIOREDOXIN | ||||||
![]() | ELECTRON TRANSPORT | ||||||
Function / homology | ![]() DNA polymerase processivity factor activity / protein-disulfide reductase activity / cell redox homeostasis / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Nikkola, M. / Gleason, F.K. / Fuchs, J.A. / Eklund, H. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 33.8 KB | Display | ![]() |
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PDB format | ![]() | 22.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 365.2 KB | Display | ![]() |
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Full document | ![]() | 364.6 KB | Display | |
Data in XML | ![]() | 3.7 KB | Display | |
Data in CIF | ![]() | 5.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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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) |
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Components
#1: Protein | Mass: 11687.321 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-CU / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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
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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 |