登録情報 データベース : PDB / ID : 1p0y 構造の表示 ダウンロードとリンクタイトル Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy 要素Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplast 詳細 キーワード TRANSFERASE / SET DOMAIN / LYSINE N-METHYLATION / MULTIPLE METHYLATION / PHOTOSYNTHESIS / POST-TRANSLATIONAL MODIFICATION機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase / [fructose-bisphosphate aldolase]-lysine N-methyltransferase / [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity / protein-lysine N-methyltransferase activity / chloroplast / methylation 類似検索 - 分子機能 Rubisco LSMT methyltransferase, plant / RBCMT, SET domain / Plant LSMT protein-lysine methyltransferase family profile. / set domain protein methyltransferase, domain 1 / set domain protein methyltransferase, domain 1 / set domain protein methyltransferase, domain 2 / Rubisco LSMT, substrate-binding domain / Rubisco LSMT, substrate-binding domain / Rubisco LSMT, substrate-binding domain superfamily / : ... Rubisco LSMT methyltransferase, plant / RBCMT, SET domain / Plant LSMT protein-lysine methyltransferase family profile. / set domain protein methyltransferase, domain 1 / set domain protein methyltransferase, domain 1 / set domain protein methyltransferase, domain 2 / Rubisco LSMT, substrate-binding domain / Rubisco LSMT, substrate-binding domain / Rubisco LSMT, substrate-binding domain superfamily / : / Rubisco LSMT substrate-binding / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / SET domain superfamily / SET domain / SET domain profile. / SET domain / Alpha-Beta Complex / Alpha Beta 類似検索 - ドメイン・相同性 N-METHYL-LYSINE / S-ADENOSYL-L-HOMOCYSTEINE / Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic 類似検索 - 構成要素生物種 Pisum sativum (エンドウ)手法 X線回折 / 分子置換 / 解像度 : 2.55 Å 詳細データ登録者 Trievel, R.C. / Flynn, E.M. / Houtz, R.L. / Hurley, J.H. 引用ジャーナル : Nat.Struct.Biol. / 年 : 2003タイトル : Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT著者 : Trievel, R.C. / Flynn, E.M. / Houtz, R.L. / Hurley, J.H. 履歴 登録 2003年4月11日 登録サイト : RCSB / 処理サイト : RCSB改定 1.0 2003年7月1日 Provider : repository / タイプ : Initial release改定 1.1 2008年4月29日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Version format compliance改定 1.3 2021年10月27日 Group : Database references / Derived calculations / カテゴリ : database_2 / struct_ref_seq_dif / struct_siteItem : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id 改定 1.4 2023年8月16日 Group : Data collection / Refinement descriptionカテゴリ : chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
すべて表示 表示を減らす Remark 999 SEQUENCE AUTHORS INFORMED THAT RESIDUES 483-488 RESULT FROM A C-TERMINAL TEV PROTEASE CLEAVAGE SITE ... SEQUENCE AUTHORS INFORMED THAT RESIDUES 483-488 RESULT FROM A C-TERMINAL TEV PROTEASE CLEAVAGE SITE THAT WAS ENGINEERED INTO THE ENZYME AFTER LEU 482. AFTER CLEAVAGE, THESE SIX RESIDUES WERE LEFT ON THE C-TERMINUS OF THIS CONSTRUCT.