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- PDB-1egr: SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE ... -

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Basic information

Entry
Database: PDB / ID: 1egr
TitleSEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN
ComponentsGLUTAREDOXIN
KeywordsELECTRON 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
Glutaredoxin, GrxA / Glutaredoxin subgroup / Glutaredoxin active site / Glutaredoxin active site. / Glutaredoxin / Glutaredoxin / Glutaredoxin domain profile. / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily ...Glutaredoxin, GrxA / Glutaredoxin subgroup / Glutaredoxin active site / Glutaredoxin active site. / Glutaredoxin / Glutaredoxin / Glutaredoxin domain profile. / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR
AuthorsSodano, 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
DepositionOct 8, 1991Processing site: BNL
Revision 1.0Oct 31, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GLUTAREDOXIN


Theoretical massNumber of molelcules
Total (without water)9,6961
Polymers9,6961
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: RESIDUE 60 IS A CIS PROLINE.
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein GLUTAREDOXIN


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

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR software
NameDeveloperClassification
DIANABRAUN,WUTHRICHrefinement
X-PLORBRUNGERrefinement
NMR ensembleConformers submitted total number: 20

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