当前蛋白身份：P01097
重新检索
差异标签只比较当前检索结果；所有PDB和assembly原始记录仍分别保留。
相关结构差异明细
一行代表一个 PDB 条目中的一个 biological assembly；同一蛋白的多个单体会分别列出。
| PDB 条目 | Assembly / 聚集状态 | 构建体 | 突变与修饰 | 配体、离子与非聚合物 | 实验方法 | 实验环境 | 结构质量 |
|---|---|---|---|---|---|---|---|
| 3ZIA The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1 提交 2013-01-07 | Assembly 1 蛋白异源复合物 异源复合物；蛋白 × 10 PDB 声明：decameric（10） 与蛋白数一致 |
链 T
23–85（63 aa）
片段：INHIBITOR PROTEIN, UNP RESIDUES 23-75
|
突变：YES | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 5 | X-RAY DIFFRACTION |
X-ray结晶条件
MICROBATCH；pH 7.5；296 K；ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O).
|
分辨率 2.50 Å R-free 0.262 |
| 3ZIA The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1 提交 2013-01-07 | Assembly 2 蛋白异源复合物 异源复合物；蛋白 × 10 PDB 声明：decameric（10） 与蛋白数一致 |
链 J
23–85（63 aa）
片段：INHIBITOR PROTEIN, UNP RESIDUES 23-75
|
突变：YES | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 EDO 1,2-ETHANEDIOL × 1 | X-RAY DIFFRACTION |
X-ray结晶条件
MICROBATCH；pH 7.5；296 K；ACTIVE F1-ATPASE (12 MG/ML) WAS EXCHANGED ON A DESALTING COLUMN INTO CRYSTALLISATION BUFFER, PREPARED IN D2O CONSISTING OF 100 MM BIS-TRIS PROPANE, PH 7.5, 100 MM SUCROSE, 1 MM ADP AND 10 MM MAGNESIUM SULPHATE. THEN THE ENZYME WAS INHIBITED AT 23C WITH A 4-FOLD MOLAR EXCESS OF YI1-53 (MUTATION E21A) IN THE PRESENCE OF 1 MM ATP AND 2 MM MAGNESIUM SULPHATE. FURTHER PORTIONS (5 UL OF A NEUTRALISED STOCK SOLUTION CONTAINING 200 MM ATP AND 400 MM MAGNESIUM SULPHATE/ML PROTEIN SOLUTION) WERE ADDED AFTER 5 AND 10 MIN. MORE THAN 95% OF THE ATP HYDROLYSIS ACTIVITY OF THE ENZYME WAS INHIBITED. SODIUM-POTASSIUM TARTRATE WAS ADDED TO 100 MM, AND THE CONCENTRATION OF THE PROTEIN SOLUTION WAS ADJUSTED TO 10 MG/ML WITH CRYSTALLISATION BUFFER. CRYSTALS WERE GROWN AT 23C IN 72 WELL MICRO-BATCH PLATES UNDER FILTERED PARAFFIN OIL. THE CRYSTALLISATION DROPS (4 UL) CONTAINED A 1:1 MIXTURE OF PROTEIN SOLUTION AND PRECIPITANT SOLUTION (20%-26% POLYETHYLENE GLYCOL 3000 AND 600 MM NACL PREPARED IN D2O).
|
分辨率 2.50 Å R-free 0.262 |