i-AAA complex / protein import into mitochondrial matrix / protein import into mitochondrial intermembrane space / 加水分解酵素; プロテアーゼ; ペプチド結合加水分解酵素; その他のペプチターゼ / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / protein maturation / mitochondrion organization / metalloendopeptidase activity / protein folding ...i-AAA complex / protein import into mitochondrial matrix / protein import into mitochondrial intermembrane space / 加水分解酵素; プロテアーゼ; ペプチド結合加水分解酵素; その他のペプチターゼ / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / protein maturation / mitochondrion organization / metalloendopeptidase activity / protein folding / mitochondrial inner membrane / mitochondrion / proteolysis / ATP binding / metal ion binding 類似検索 - 分子機能
Peptidase M41 / Peptidase, FtsH / Peptidase M41-like / Peptidase family M41 / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core ...Peptidase M41 / Peptidase, FtsH / Peptidase M41-like / Peptidase family M41 / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
Protein chi angle constraints total count: 47 / Protein other angle constraints total count: 34 / Protein phi angle constraints total count: 85 / Protein psi angle constraints total count: 94
代表構造
選択基準: minimized average structure
NMRアンサンブル
コンフォーマー選択の基準: structures with the least restraint violations 計算したコンフォーマーの数: 100 / 登録したコンフォーマーの数: 23 / Maximum lower distance constraint violation: 0.02 Å / Maximum torsion angle constraint violation: 0.3 ° / Maximum upper distance constraint violation: 0.08 Å
NMR ensemble rms
Distance rms dev: 0.013 Å / Distance rms dev error: 0.001 Å