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2PE6

Non-covalent complex between human SUMO-1 and human Ubc9

2PE6 の概要
エントリーDOI10.2210/pdb2pe6/pdb
関連するPDBエントリー1A3S
分子名称SUMO-conjugating enzyme UBC9, Small ubiquitin-related modifier 1 (3 entities in total)
機能のキーワードsumo, ubiquitin-like, conjugation, smt3, ubc9, protein binding, ligase
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Nucleus: P63279
Nucleus membrane: P63165
タンパク質・核酸の鎖数2
化学式量合計29462.64
構造登録者
Capili, A.D.,Lima, C.D. (登録日: 2007-04-02, 公開日: 2007-04-17, 最終更新日: 2023-08-30)
主引用文献Capili, A.D.,Lima, C.D.
Structure and Analysis of a Complex between SUMO and Ubc9 Illustrates Features of a Conserved E2-Ubl Interaction.
J.Mol.Biol., 369:608-618, 2007
Cited by
PubMed Abstract: The SUMO E2 Ubc9 serves as a lynchpin in the SUMO conjugation pathway, interacting with the SUMO E1 during activation, with thioester linked SUMO after E1 transfer and with the substrate and SUMO E3 ligases during conjugation. Here, we describe the structure determination of a non-covalent complex between human Ubc9 and SUMO-1 at 2.4 A resolution. Non-covalent interactions between Ubc9 and SUMO are conserved in human and yeast insomuch as human Ubc9 interacts with each of the human SUMO isoforms, and yeast Ubc9 interacts with Smt3, the yeast SUMO ortholog. Structural comparisons reveal similarities to several other non-covalent complexes in the ubiquitin pathway, suggesting that the non-covalent Ubc9-SUMO interface may be important for poly-SUMO chain formation, for E2 recruitment to SUMO conjugated substrates, or for mediating E2 interactions with either E1 or E3 ligases. Biochemical analysis suggests that this surface is less important for E1 activation or di-SUMO-2 formation, but more important for E3 interactions and for poly-SUMO chain formation when the chain exceeds more than two SUMO proteins.
PubMed: 17466333
DOI: 10.1016/j.jmb.2007.04.006
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 2pe6
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2026-07-08に公開中

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