登録情報 | データベース: PDB / ID: 2qc7 |
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タイトル | Crystal structure of the protein-disulfide isomerase related chaperone ERp29 |
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要素 | Endoplasmic reticulum protein ERp29 |
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キーワード | CHAPERONE / b domain (residues 33-153) / D domain (residues 154-261) |
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機能・相同性 | 機能・相同性情報
regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / protein secretion / protein unfolding / smooth endoplasmic reticulum / negative regulation of protein secretion / transport vesicle / intracellular protein transport / positive regulation of MAP kinase activity / melanosome / protein folding ...regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / protein secretion / protein unfolding / smooth endoplasmic reticulum / negative regulation of protein secretion / transport vesicle / intracellular protein transport / positive regulation of MAP kinase activity / melanosome / protein folding / protein-folding chaperone binding / positive regulation of protein phosphorylation / endoplasmic reticulum lumen / negative regulation of gene expression / positive regulation of gene expression / cell surface / endoplasmic reticulum / protein homodimerization activity / membrane類似検索 - 分子機能 Endoplasmic reticulum protein erp29 / Endoplasmic reticulum resident protein 29, C-terminal domain / Endoplasmic reticulum resident protein 29, C-terminal / ERp29, N-terminal / Endoplasmic reticulum resident protein 29 / Endoplasmic reticulum resident protein 29, C-terminal domain superfamily / Endoplasmic reticulum protein ERp29, C-terminal domain / ERp29, N-terminal domain / Endoplasmic reticulum targeting sequence. / Glutaredoxin ...Endoplasmic reticulum protein erp29 / Endoplasmic reticulum resident protein 29, C-terminal domain / Endoplasmic reticulum resident protein 29, C-terminal / ERp29, N-terminal / Endoplasmic reticulum resident protein 29 / Endoplasmic reticulum resident protein 29, C-terminal domain superfamily / Endoplasmic reticulum protein ERp29, C-terminal domain / ERp29, N-terminal domain / Endoplasmic reticulum targeting sequence. / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / Up-down Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta類似検索 - ドメイン・相同性 |
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生物種 | Homo sapiens (ヒト) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.9 Å |
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データ登録者 | Barak, N.N. / Sevvana, M. / Neumann, P. / Malesevic, M. / Naumann, K. / Fischer, G. / Sheldrick, G.M. / Stubbs, M.T. / Ferrari, D.M. |
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引用 | ジャーナル: J.Mol.Biol. / 年: 2009 タイトル: Crystal structure and functional analysis of the protein disulfide isomerase-related protein ERp29. 著者: Barak, N.N. / Neumann, P. / Sevvana, M. / Schutkowski, M. / Naumann, K. / Malesevic, M. / Reichardt, H. / Fischer, G. / Stubbs, M.T. / Ferrari, D.M. |
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履歴 | 登録 | 2007年6月19日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2008年6月24日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2011年7月13日 | Group: Advisory / Version format compliance |
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改定 1.2 | 2023年8月30日 | Group: Data collection / Database references / Refinement description カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_source / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_ref_seq_dif Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ref_seq_dif.details |
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