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- PDB-1xob: THIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1xob
TitleTHIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURES
ComponentsTHIOREDOXIN
KeywordsELECTRON TRANSPORT / REDOX-ACTIVE CENTER
Function / homology
Function and homology information


DNA polymerase processivity factor activity / protein-disulfide reductase activity / cell redox homeostasis / cytoplasm / cytosol
Similarity search - Function
Thioredoxin / Thioredoxin / Thioredoxin, conserved site / Thioredoxin family active site. / Thioredoxin domain profile. / Thioredoxin domain / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR
AuthorsJeng, M.-F. / Campbell, A.P. / Begley, T. / Holmgren, A. / Case, D.A. / Wright, P.E. / Dyson, H.J.
Citation
Journal: Structure / Year: 1994
Title: High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin.
Authors: Jeng, M.F. / Campbell, A.P. / Begley, T. / Holmgren, A. / Case, D.A. / Wright, P.E. / Dyson, H.J.
#1: Journal: J.Biomol.NMR / Year: 1994
Title: Effect of Disulfide Bridge Formation on the NMR Spectrum of a Protein: Studies on Oxidized and Reduced Escherichia Coli Thioredoxin
Authors: Chandrasekhar, K. / Campbell, A.P. / Jeng, M.F. / Holmgren, A. / Dyson, H.J.
#2: Journal: FEBS Lett. / Year: 1991
Title: Assignment of the 15N NMR Spectra of Reduced and Oxidized Escherichia Coli Thioredoxin
Authors: Chandrasekhar, K. / Krause, G. / Holmgren, A. / Dyson, H.J.
#3: Journal: Biochemistry / Year: 1990
Title: Three-Dimensional Solution Structure of the Reduced Form of Escherichia Coli Thioredoxin Determined by Nuclear Magnetic Resonance Spectroscopy
Authors: Dyson, H.J. / Gippert, G.P. / Case, D.A. / Holmgren, A. / Wright, P.E.
#4: Journal: Biochemistry / Year: 1989
Title: Assignment of the Proton NMR Spectrum of Reduced and Oxidized Thioredoxin: Sequence-Specific Assignments, Secondary Structure, and Global Fold
Authors: Dyson, H.J. / Holmgren, A. / Wright, P.E.
History
DepositionNov 28, 1995Processing site: BNL
SupersessionJun 10, 1996ID: 1TRX
Revision 1.0Jun 10, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4May 1, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: THIOREDOXIN


Theoretical massNumber of molelcules
Total (without water)11,6871
Polymers11,6871
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein THIOREDOXIN / TRX-SH2


Mass: 11687.388 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: REDUCED DITHIO FORM / Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PBHK8 / Production host: Escherichia coli (E. coli) / Strain (production host): C1A / References: UniProt: P0AA25

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other

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Processing

SoftwareName: AMBER / Classification: refinement
NMR softwareName: Amber
Developer: PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
Classification: refinement
NMR ensembleConformers submitted total number: 20

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