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1jhb

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Revision as of 07:19, 14 April 2021

HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES

Structural highlights

1jhb is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLRX1_HUMAN] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The determination of the nuclear magnetic resonance (NMR) solution structure of fully reduced human glutaredoxin is described. A total of 1159 useful nuclear Overhauser effect (NOE) upper distance constraints and 187 dihedral angle constraints were obtained as the input for the structure calculations for which the torsion angle dynamics program DYANA has been utilized followed by energy minimization in water with the AMBER force field as implemented in the program OPAL. The resulting 20 conformers have an average root-mean-square deviation value relative to the mean coordinates of 0.54 A for all the backbone atoms N, Calpha and C', and of 1.01 A for all heavy atoms. Human glutaredoxin consists of a four-stranded mixed beta-sheet composed of residues 15 to 19, 43 to 47, 72 to 75 and 78 to 81, and five alpha-helices composed of residues 4 to 9, 24 to 34, 54 to 65, 83 to 91, and 94 to 100. Comparisons with the structures of Escherichia coli glutaredoxin-1, pig liver glutaredoxin and human thioredoxin were made. Electrostatic calculations on the human glutaredoxin structure and that of related proteins provide an understanding of the variation of pKa values for the nucleophilic cysteine in the active site observed among these proteins. In addition, the high-resolution NMR solution structure of human glutaredoxin has been used to model the binding site for glutathione and for ribonucleotide reductase B1 by molecular dynamics simulations.

The NMR solution structure of human glutaredoxin in the fully reduced form.,Sun C, Berardi MJ, Bushweller JH J Mol Biol. 1998 Jul 24;280(4):687-701. PMID:9677297^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sun C, Berardi MJ, Bushweller JH. The NMR solution structure of human glutaredoxin in the fully reduced form. J Mol Biol. 1998 Jul 24;280(4):687-701. PMID:9677297 doi:10.1006/jmbi.1998.1913

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jhb"

@@ Line 3: / Line 3: @@
 <StructureSection load='1jhb' size='340' side='right'caption='[[1jhb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jhb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JHB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jhb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JHB FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jhb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jhb OCA], [http://pdbe.org/1jhb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jhb RCSB], [http://www.ebi.ac.uk/pdbsum/1jhb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jhb ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jhb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jhb OCA], [https://pdbe.org/1jhb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jhb RCSB], [https://www.ebi.ac.uk/pdbsum/1jhb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jhb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GLRX1_HUMAN GLRX1_HUMAN]] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
+[[https://www.uniprot.org/uniprot/GLRX1_HUMAN GLRX1_HUMAN]] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1jhb

From Proteopedia

Revision as of 07:19, 14 April 2021

HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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