- PDB-1ux9: Mapping protein matrix cavities in human cytoglobin through Xe at... -
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基本情報
登録情報
データベース: PDB / ID: 1ux9
タイトル
Mapping protein matrix cavities in human cytoglobin through Xe atom binding: a crystallographic investigation
要素
CYTOGLOBIN
キーワード
OXYGEN TRANSPORT (血液) / OXYGEN STORAGE/TRANSPORT / HEME (ヘム) / TRANSPORT
機能・相同性
機能・相同性情報
Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor / fatty acid peroxidase activity / nitric oxide dioxygenase activity, heme protein as donor / negative regulation of hepatic stellate cell activation / Intracellular oxygen transport / nitric oxide catabolic process / negative regulation of collagen biosynthetic process / carbon monoxide binding / negative regulation of fibroblast migration / catalase activity ...Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor / fatty acid peroxidase activity / nitric oxide dioxygenase activity, heme protein as donor / negative regulation of hepatic stellate cell activation / Intracellular oxygen transport / nitric oxide catabolic process / negative regulation of collagen biosynthetic process / carbon monoxide binding / negative regulation of fibroblast migration / catalase activity / スーパーオキシドディスムターゼ / superoxide dismutase activity / Β酸化 / nitrite reductase activity / 酸化還元酵素; 他の含窒素化合物が電子供与する / 血液 / 酸化還元酵素; 過酸化物を電子受容体にする; ペルオキシダーゼ / eNOS activation / removal of superoxide radicals / oxygen carrier activity / peroxidase activity / oxygen binding / response to oxidative stress / oxidoreductase activity / response to hypoxia / neuron projection / iron ion binding / neuronal cell body / heme binding / 細胞核 / 細胞質基質 / 細胞質 類似検索 - 分子機能
ENGINEERED MUTATION IN CHAIN A, CYS 38 TO SER 38 ENGINEERED MUTATION IN CHAIN A, CYS 83 TO SER 83 ...ENGINEERED MUTATION IN CHAIN A, CYS 38 TO SER 38 ENGINEERED MUTATION IN CHAIN A, CYS 83 TO SER 83 ENGINEERED MUTATION IN CHAIN B, CYS 38 TO SER 38 ENGINEERED MUTATION IN CHAIN B, CYS 83 TO SER 83