登録情報 | データベース: PDB / ID: 3b9p |
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タイトル | Spastin |
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要素 | CG5977-PA, isoform A |
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キーワード | HYDROLASE / AAA ATPase / ATP-binding / Nucleotide-binding |
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機能・相同性 | 機能・相同性情報
positive regulation of axon extension involved in regeneration / hemocyte migration / negative regulation of synaptic assembly at neuromuscular junction / Sealing of the nuclear envelope (NE) by ESCRT-III / negative regulation of neuromuscular synaptic transmission / positive regulation of neuromuscular synaptic transmission / microtubule-severing ATPase / positive regulation of synaptic assembly at neuromuscular junction / microtubule severing ATPase activity / mitotic chromosome movement towards spindle pole ...positive regulation of axon extension involved in regeneration / hemocyte migration / negative regulation of synaptic assembly at neuromuscular junction / Sealing of the nuclear envelope (NE) by ESCRT-III / negative regulation of neuromuscular synaptic transmission / positive regulation of neuromuscular synaptic transmission / microtubule-severing ATPase / positive regulation of synaptic assembly at neuromuscular junction / microtubule severing ATPase activity / mitotic chromosome movement towards spindle pole / microtubule severing / positive regulation of lipid metabolic process / regulation of terminal button organization / positive regulation of microtubule depolymerization / mitotic spindle elongation / negative regulation of microtubule depolymerization / protein hexamerization / positive regulation of dendrite morphogenesis / transmission of nerve impulse / mitotic sister chromatid segregation / alpha-tubulin binding / cytoplasmic microtubule organization / lipid droplet / adult locomotory behavior / isomerase activity / locomotory behavior / neuromuscular junction / regulation of synaptic plasticity / terminal bouton / microtubule cytoskeleton organization / spindle / chromosome / microtubule cytoskeleton / nervous system development / microtubule binding / microtubule / membrane => GO:0016020 / cell division / centrosome / ATP hydrolysis activity / ATP binding / membrane / nucleus / cytoplasm類似検索 - 分子機能 Spastin / Vps4 oligomerisation, C-terminal / : / MIT domain / Microtubule Interacting and Trafficking molecule domain / Vps4 C terminal oligomerisation domain / Helicase, Ruva Protein; domain 3 - #60 / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site ...Spastin / Vps4 oligomerisation, C-terminal / : / MIT domain / Microtubule Interacting and Trafficking molecule domain / Vps4 C terminal oligomerisation domain / Helicase, Ruva Protein; domain 3 - #60 / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / Helicase, Ruva Protein; domain 3 / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / Orthogonal 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 | ![](img/tx_arthropod.gif) Drosophila melanogaster (キイロショウジョウバエ) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.7 Å |
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データ登録者 | Roll-Mecak, A. / Vale, R.D. |
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引用 | ジャーナル: Nature / 年: 2008 タイトル: Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. 著者: Roll-Mecak, A. / Vale, R.D. |
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履歴 | 登録 | 2007年11月6日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2008年1月22日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2011年7月13日 | Group: Version format compliance |
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改定 1.2 | 2024年2月21日 | Group: Data collection / Database references / Derived calculations カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site Item: _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 |
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