登録情報 データベース : PDB / ID : 2c78 構造の表示 ダウンロードとリンクタイトル EF-Tu complexed with a GTP analog and the antibiotic pulvomycin 要素ELONGATION FACTOR TU-A 詳細 キーワード HYDROLASE / GTPASE / TRANSLATION ELONGATION FACTOR / PROTEIN SYNTHESIS / ANTIBIOTIC / GTP-BINDING / NUCLEOTIDE-BINDING / PHOSPHORYLATION / PROTEIN BIOSYNTHESIS / ELONGATION FACTOR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
translation elongation factor activity / GTPase activity / GTP binding / RNA binding / cytosol 類似検索 - 分子機能 Translation elongation factor EFTu/EF1A, bacterial/organelle / Elongation factor Tu, domain 2 / Elongation factor Tu (EF-Tu), GTP-binding domain / : / Translation elongation factor EFTu/EF1A, C-terminal / Elongation factor Tu C-terminal domain / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Tr-type G domain, conserved site / Translational (tr)-type guanine nucleotide-binding (G) domain signature. ... Translation elongation factor EFTu/EF1A, bacterial/organelle / Elongation factor Tu, domain 2 / Elongation factor Tu (EF-Tu), GTP-binding domain / : / Translation elongation factor EFTu/EF1A, C-terminal / Elongation factor Tu C-terminal domain / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Tr-type G domain, conserved site / Translational (tr)-type guanine nucleotide-binding (G) domain signature. / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Elongation Factor Tu (Ef-tu); domain 3 / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Small GTP-binding protein domain / Translation protein, beta-barrel domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Beta Barrel / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta 類似検索 - ドメイン・相同性 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Chem-PUL / Elongation factor Tu-A 類似検索 - 構成要素生物種 THERMUS THERMOPHILUS (バクテリア)手法 X線回折 / シンクロトロン / 分子置換 / 解像度 : 1.4 Å 詳細データ登録者 Parmeggiani, A. / Krab, I.M. / Okamura, S. / Nielsen, R.C. / Nyborg, J. / Nissen, P. 引用ジャーナル : Biochemistry / 年 : 2006タイトル : Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu.著者 : Parmeggiani, A. / Krab, I.M. / Okamura, S. / Nielsen, R.C. / Nyborg, J. / Nissen, P. 履歴 登録 2005年11月18日 登録サイト : PDBE / 処理サイト : PDBE改定 1.0 2006年3月16日 Provider : repository / タイプ : Initial release改定 1.1 2011年5月8日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Version format compliance改定 1.3 2018年3月28日 Group : Database references / Source and taxonomy / カテゴリ : citation / entity_src_genItem : _citation.page_last / _citation.pdbx_database_id_DOI ... _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant 改定 1.4 2019年7月24日 Group : Data collection / カテゴリ : diffrn_source / Item : _diffrn_source.pdbx_synchrotron_site改定 1.5 2023年12月13日 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description / Structure summary カテゴリ : chem_comp / chem_comp_atom ... chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_database_status / pdbx_entity_nonpoly / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn Item : _chem_comp.name / _database_2.pdbx_DOI ... _chem_comp.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
すべて表示 表示を減らす Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.