+Open data
-Basic information
Entry | Database: PDB / ID: 1grx | ||||||
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Title | STRUCTURE OF E. 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 | Bushweller, J.H. / Billeter, M. / Holmgren, L.A. / Wuthrich, K. | ||||||
Citation | Journal: Protein Sci. / Year: 1992 Title: NMR structure of oxidized Escherichia 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. #1: Journal: J.Mol.Biol. / Year: 1991 Title: Sequence-Specific 1H NMR Assignments and Determination of the Three-Dimensional Structure of Reduced E. Coli Glutaredoxin Authors: Sodano, P. / Xia, T.H. / Bushweller, J.H. / Bjornberg, O. / Holmgren, A. / Billeter, M. / Wuthrich, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1grx.cif.gz | 594.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1grx.ent.gz | 524.2 KB | Display | PDB format |
PDBx/mmJSON format | 1grx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gr/1grx ftp://data.pdbj.org/pub/pdb/validation_reports/gr/1grx | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9679.759 Da / Num. of mol.: 1 / Mutation: C14S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: STRAIN N4830/PAHOB1[C14->S] / References: UniProt: P68688 |
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#2: Chemical | ChemComp-GSH / |
-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
NMR software | Name: DIANA / Developer: GUNTERT,BRAUN,WUTHRICH / Classification: refinement |
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NMR ensemble | Conformers submitted total number: 20 |