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Yorodumi- PDB-1egr: SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE ... -
+Open data
-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 | ||||||
Components | GLUTAREDOXIN | ||||||
Keywords | ELECTRON TRANSPORT | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Sodano, P. / Xia, T.-H. / Bushweller, J.H. / Bjornberg, O. / Holmgren, A. / Billeter, M. / Wuthrich, K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1991 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: Journal: Protein Sci. / Year: 1992 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: Journal: Eur.J.Biochem. / Year: 1991 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: Journal: Protein Expr.Purif. / Year: 1991 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1egr.cif.gz | 580.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1egr.ent.gz | 495.6 KB | Display | PDB format |
PDBx/mmJSON format | 1egr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eg/1egr ftp://data.pdbj.org/pub/pdb/validation_reports/eg/1egr | 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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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.) Escherichia coli (E. coli) / References: UniProt: P68688 |
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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
Software |
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NMR software |
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NMR ensemble | Conformers submitted total number: 20 |