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1TOF

THIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURES

1TOF の概要
エントリーDOI10.2210/pdb1tof/pdb
分子名称THIOREDOXIN H (1 entity in total)
機能のキーワードoxidoreductase, electron transport
由来する生物種Chlamydomonas reinhardtii
細胞内の位置Cytoplasm: P80028
タンパク質・核酸の鎖数1
化学式量合計11727.53
構造登録者
Mittard, V.,Blackledge, M.J.,Stein, M.,Jacquot, J.-P.,Marion, D.,Lancelin, J.-M. (登録日: 1996-05-30, 公開日: 1996-12-07, 最終更新日: 2024-10-30)
主引用文献Mittard, V.,Blackledge, M.J.,Stein, M.,Jacquot, J.P.,Marion, D.,Lancelin, J.M.
NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii.
Eur.J.Biochem., 243:374-383, 1997
Cited by
PubMed Abstract: NMR solution structures of a cytosolic plant thioredoxin h (112 amino acids, 11.7 kDa) from the green alga Chlamydonmonas reinhardtii have been calculated on the basis of 1904 NMR distance restraints, which include 90 distances used to restrain 45 hydrogen bonds, and 44 phi dihedral restraints. The structure of C. reinhardtii thioredoxin h was solved in its oxidised form, and the ensemble of 23 converged structures superpose to the geometric average structure with an atomic rmsd of 0.080 nm +/- 0.016 for the (N, C(alpha), C) backbone atoms of residues 4-110. Comparisons with other thioredoxins, such as thioredoxin from the bacterium Escherichia coli, thioredoxin 2 from a cyanobacterium of the Anabaena genus, and human thioredoxin, showed that thioredoxin h models share more structural features with human thioredoxin than with other bacterial thioredoxins. Examination of the accessible surface around the redoxactive peptide sequence indicates that a potent thioredoxin-h-substrate interaction could be similar to the vertebrate thioredoxin-substrate interactions.
PubMed: 9030762
DOI: 10.1111/j.1432-1033.1997.0374a.x
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1tof
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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