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- PDB-1egr: SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1egr | ||||||
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Title | SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN | ||||||
![]() | GLUTAREDOXIN | ||||||
![]() | ELECTRON TRANSPORT | ||||||
Function / homology | ![]() cysteine biosynthetic process via S-sulfo-L-cysteine / sulfate assimilation via adenylyl sulfate reduction / protein-disulfide reductase (glutathione) activity / glutathione disulfide oxidoreductase activity / disulfide oxidoreductase activity / deoxyribonucleotide biosynthetic process / protein-disulfide reductase activity / cell redox homeostasis / cellular response to oxidative stress / electron transfer activity ...cysteine biosynthetic process via S-sulfo-L-cysteine / sulfate assimilation via adenylyl sulfate reduction / protein-disulfide reductase (glutathione) activity / glutathione disulfide oxidoreductase activity / disulfide oxidoreductase activity / deoxyribonucleotide biosynthetic process / protein-disulfide reductase activity / cell redox homeostasis / cellular response to oxidative stress / electron transfer activity / nucleotide binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Sodano, P. / Xia, T.-H. / Bushweller, J.H. / Bjornberg, O. / Holmgren, A. / Billeter, M. / Wuthrich, K. | ||||||
![]() | ![]() Title: Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin. Authors: Sodano, P. / Xia, T.H. / Bushweller, J.H. / Bjornberg, O. / Holmgren, A. / Billeter, M. / Wuthrich, K. #1: ![]() Title: The NMR Structure of Oxidized E. Coli Glutaredoxin. Comparison with Reduced E. Coli Glutaredoxin and Functionally Related Proteins Authors: Xia, T.-H. / Bushweller, J.H. / Sodano, P. / Billeter, M. / Bjornberg, O. / Holmgren, A. / Wuthrich, K. #2: ![]() Title: Nuclear Magnetic Resonance Studies of Recombinant Escherichia Coli Glutaredoxin: Sequence-Specific Assignments and Secondary Structure Determination for the Oxidized Form Authors: Sodano, P. / Chary, K.V.R. / Bjornberg, O. / Holmgren, A. / Kren, B. / Fuchs, J.A. / Wuthrich, K. #3: ![]() Title: Characterization of Homogeneous Recombinant Glutaredoxin from Escherichia Coli: Purification from an Inducible Lambda-P(L) Expression System and Properties of a Novel Elongated Form Protein ...Title: Characterization of Homogeneous Recombinant Glutaredoxin from Escherichia Coli: Purification from an Inducible Lambda-P(L) Expression System and Properties of a Novel Elongated Form Protein Expression and Purification Authors: Bjornberg, O. / Holmgren, A. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 580.4 KB | Display | ![]() |
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PDB format | ![]() | 495.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 352.9 KB | Display | ![]() |
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Full document | ![]() | 495.4 KB | Display | |
Data in XML | ![]() | 31.2 KB | Display | |
Data in CIF | ![]() | 51.8 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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Atom site foot note | 1: RESIDUE 60 IS A CIS PROLINE. | |||||||||
NMR ensembles |
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Components
#1: Protein | Mass: 9695.823 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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NMR software |
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NMR ensemble | Conformers submitted total number: 20 |