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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 1bka | ||||||
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タイトル | OXALATE-SUBSTITUTED DIFERRIC LACTOFERRIN | ||||||
![]() | LACTOFERRIN | ||||||
![]() | IRON BINDING PROTEIN / ANION BINDING | ||||||
機能・相同性 | ![]() host-mediated suppression of viral proces / membrane destabilizing activity / Mtb iron assimilation by chelation / phagocytic vesicle lumen / positive regulation of toll-like receptor 4 signaling pathway / Metal sequestration by antimicrobial proteins / negative regulation of viral process / negative regulation of tumor necrosis factor (ligand) superfamily member 11 production / negative regulation of single-species biofilm formation in or on host organism / positive regulation of bone mineralization involved in bone maturation ...host-mediated suppression of viral proces / membrane destabilizing activity / Mtb iron assimilation by chelation / phagocytic vesicle lumen / positive regulation of toll-like receptor 4 signaling pathway / Metal sequestration by antimicrobial proteins / negative regulation of viral process / negative regulation of tumor necrosis factor (ligand) superfamily member 11 production / negative regulation of single-species biofilm formation in or on host organism / positive regulation of bone mineralization involved in bone maturation / negative regulation of osteoclast development / antifungal humoral response / specific granule / negative regulation of lipopolysaccharide-mediated signaling pathway / positive regulation of chondrocyte proliferation / negative regulation of ATP-dependent activity / regulation of tumor necrosis factor production / bone morphogenesis / Antimicrobial peptides / negative regulation of viral genome replication / positive regulation of osteoblast proliferation / humoral immune response / 加水分解酵素; プロテアーゼ; ペプチド結合加水分解酵素; セリンエンドペプチターゼ / cysteine-type endopeptidase inhibitor activity / positive regulation of protein serine/threonine kinase activity / positive regulation of osteoblast differentiation / regulation of cytokine production / ossification / innate immune response in mucosa / protein serine/threonine kinase activator activity / secretory granule / lipopolysaccharide binding / recycling endosome / specific granule lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / positive regulation of NF-kappaB transcription factor activity / antibacterial humoral response / tertiary granule lumen / heparin binding / iron ion transport / defense response to Gram-negative bacterium / killing of cells of another organism / positive regulation of canonical NF-kappaB signal transduction / early endosome / iron ion binding / Amyloid fiber formation / serine-type endopeptidase activity / Neutrophil degranulation / negative regulation of apoptotic process / cell surface / protein-containing complex / proteolysis / DNA binding / extracellular space / extracellular exosome / extracellular region / nucleus / plasma membrane / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() ![]() | ||||||
![]() | Baker, H.M. / Smith, C.A. / Baker, E.N. | ||||||
![]() | ![]() タイトル: Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin. 著者: Baker, H.M. / Anderson, B.F. / Brodie, A.M. / Shongwe, M.S. / Smith, C.A. / Baker, E.N. #1: ![]() タイトル: Structure of Human Diferric Lactoferrin Refined at 2.2 Angstroms Resolution 著者: Haridas, M. / Anderson, B.F. / Baker, E.N. #2: ![]() タイトル: Anion Binding by Human Lactoferrin: Results from Crystallographic and Physicochemical Studies 著者: Shongwe, M.S. / Smith, C.A. / Ainscough, E.W. / Baker, H.M. / Brodie, A.M. / Baker, E.N. #3: ![]() タイトル: Structure of Human Lactoferrin: Crystallographic Structure Analysis and Refinement at 2.8 A Resolution 著者: Anderson, B.F. / Baker, H.M. / Norris, G.E. / Rice, D.W. / Baker, E.N. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 153.4 KB | 表示 | ![]() |
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PDB形式 | ![]() | 115.6 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 420.1 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 497.3 KB | 表示 | |
XML形式データ | ![]() | 26.8 KB | 表示 | |
CIF形式データ | ![]() | 37.5 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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単位格子 |
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要素
#1: タンパク質 | 分子量: 76263.266 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() | ||||||
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#2: 化合物 | #3: 化合物 | #4: 水 | ChemComp-HOH / | Has protein modification | Y | |
-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶 | マシュー密度: 2.76 Å3/Da / 溶媒含有率: 53 % | ||||||||||||||||||||
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結晶化 | *PLUS 温度: 4 ℃ / pH: 8 / 手法: microdialysis | ||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
放射光源 | 由来: ![]() ![]() ![]() |
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検出器 | タイプ: RIGAKU / 検出器: IMAGE PLATE / 日付: 1993年3月15日 |
放射 | 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
放射波長 | 波長: 1 Å / 相対比: 1 |
反射 | Num. obs: 31874 / % possible obs: 99 % / Observed criterion σ(I): 3 / 冗長度: 4.3 % / Rmerge(I) obs: 0.115 |
反射 | *PLUS 最高解像度: 2.4 Å |
反射 シェル | *PLUS 最高解像度: 2.4 Å / 最低解像度: 2.54 Å / % possible obs: 83.3 % |
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解析
ソフトウェア |
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精密化 | 解像度: 2.4→8 Å / Num. reflection obs: 31758 / σ(F): 0 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 解像度: 2.4→8 Å
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拘束条件 |
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ソフトウェア | *PLUS 名称: PROLSQ / 分類: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化 | *PLUS Rfactor obs: 0.196 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
溶媒の処理 | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | *PLUS |