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2CYX

Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)

2CYX の概要
エントリーDOI10.2210/pdb2cyx/pdb
分子名称Ubiquitin-conjugating enzyme E2 G2 (2 entities in total)
機能のキーワードubiquitin-conjugating enzyme (e2), ubl conjugation pathway, ligase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数3
化学式量合計57179.20
構造登録者
主引用文献Arai, R.,Yoshikawa, S.,Murayama, K.,Imai, Y.,Takahashi, R.,Shirouzu, M.,Yokoyama, S.
Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)
Acta Crystallogr.,Sect.F, 62:330-334, 2006
Cited by
PubMed Abstract: The human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7) is involved in protein degradation, including a process known as endoplasmic reticulum-associated degradation (ERAD). The crystal structure of human UBE2G2/UBC7 was solved at 2.56 angstroms resolution. The UBE2G2 structure comprises a single domain consisting of an antiparallel beta-sheet with four strands, five alpha-helices and two 3(10)-helices. Structural comparison of human UBE2G2 with yeast Ubc7 indicated that the overall structures are similar except for the long loop region and the C-terminal helix. Superimposition of UBE2G2 on UbcH7 in a c-Cbl-UbcH7-ZAP70 ternary complex suggested that the two loop regions of UBE2G2 interact with the RING domain in a similar way to UbcH7. In addition, the extra loop region of UBE2G2 may interact with the RING domain or its neighbouring region and may be involved in the binding specificity and stability.
PubMed: 16582478
DOI: 10.1107/S1744309106009006
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.56 Å)
構造検証レポート
Validation report summary of 2cyx
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2026-02-11に公開中

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