登録情報 | データベース: PDB / ID: 2qtl |
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タイトル | Crystal Structure of the FAD-containing FNR-like Module of Human Methionine Synthase Reductase |
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要素 | Methionine synthase reductase |
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キーワード | OXIDOREDUCTASE / alpha-beta-alpha structural motif / flattened antiparallel beta barrel / flexible hinge region / connecting domain / FAD-binding region |
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機能・相同性 | 機能・相同性情報
[methionine synthase] reductase / [methionine synthase] reductase (NADPH) activity / negative regulation of cystathionine beta-synthase activity / Defective MTRR causes HMAE / Defective MTR causes HMAG / oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor / Sulfur amino acid metabolism / Cobalamin (Cbl) metabolism / homocysteine catabolic process / homocysteine metabolic process ...[methionine synthase] reductase / [methionine synthase] reductase (NADPH) activity / negative regulation of cystathionine beta-synthase activity / Defective MTRR causes HMAE / Defective MTR causes HMAG / oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor / Sulfur amino acid metabolism / Cobalamin (Cbl) metabolism / homocysteine catabolic process / homocysteine metabolic process / S-adenosylmethionine cycle / Methylation / methionine biosynthetic process / NADPH-hemoprotein reductase activity / intermediate filament cytoskeleton / folic acid metabolic process / NADPH binding / FAD binding / FMN binding / flavin adenine dinucleotide binding / nucleoplasm / cytosol類似検索 - 分子機能 NADPH-cytochrome p450 Reductase; Chain A, domain 3 / NADPH-cytochrome p450 Reductase; Chain A, domain 3 / Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module / Translation factors / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / FAD binding domain / Flavodoxin-like / Elongation Factor Tu (Ef-tu); domain 3 / Flavoprotein pyridine nucleotide cytochrome reductase ...NADPH-cytochrome p450 Reductase; Chain A, domain 3 / NADPH-cytochrome p450 Reductase; Chain A, domain 3 / Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module / Translation factors / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / FAD binding domain / Flavodoxin-like / Elongation Factor Tu (Ef-tu); domain 3 / Flavoprotein pyridine nucleotide cytochrome reductase / Flavodoxin / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / Oxidoreductase FAD/NAD(P)-binding / Oxidoreductase NAD-binding domain / FAD-binding domain, ferredoxin reductase-type / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / Ferredoxin reductase-type FAD binding domain profile. / Riboflavin synthase-like beta-barrel / Flavoprotein-like superfamily / Up-down Bundle / Beta Barrel / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta類似検索 - ドメイン・相同性 FLAVIN-ADENINE DINUCLEOTIDE / Methionine synthase reductase類似検索 - 構成要素 |
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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: 1.9 Å |
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データ登録者 | Wolthers, K.R. / Lou, X. / Toogood, H.S. / Leys, D. / Scrutton, N.S. |
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引用 | ジャーナル: Biochemistry / 年: 2007 タイトル: Mechanism of Coenzyme Binding to Human Methionine Synthase Reductase Revealed through the Crystal Structure of the FNR-like Module and Isothermal Titration Calorimetry 著者: Wolthers, K.R. / Lou, X. / Toogood, H.S. / Leys, D. / Scrutton, N.S. |
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履歴 | 登録 | 2007年8月2日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2007年11月13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 | 2017年10月25日 | Group: Advisory / Refinement description / カテゴリ: pdbx_unobs_or_zero_occ_atoms / software |
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改定 1.3 | 2022年12月21日 | Group: Advisory / Database references / Derived calculations カテゴリ: database_2 / pdbx_unobs_or_zero_occ_atoms ...database_2 / pdbx_unobs_or_zero_occ_atoms / struct_conn / 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_conn.pdbx_leaving_atom_flag / _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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