[English] 日本語
![](img/lk-miru.gif)
- PDB-1ego: NMR STRUCTURE OF OXIDIZED ESCHERICHIA COLI GLUTAREDOXIN: COMPARIS... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1ego | ||||||
---|---|---|---|---|---|---|---|
Title | NMR STRUCTURE OF OXIDIZED ESCHERICHIA COLI GLUTAREDOXIN: COMPARISON WITH REDUCED E. COLI GLUTAREDOXIN AND FUNCTIONALLY RELATED PROTEINS | ||||||
![]() | 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 | ||||||
![]() | Xia, T.-H. / Bushweller, J.H. / Sodano, P. / Billeter, M. / Bjornberg, O. / Holmgren, A. / Wuthrich, K. | ||||||
![]() | ![]() 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: ![]() 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. #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. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 578.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 510 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 354.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 504.9 KB | Display | |
Data in XML | ![]() | 32.9 KB | Display | |
Data in CIF | ![]() | 53.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
Atom site foot note | 1: RESIDUE 60 IS A CIS PROLINE. | |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 9695.823 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|
-
Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
---|
-
Processing
Software |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
NMR software |
| |||||||||
NMR ensemble | Conformers submitted total number: 20 |