当前蛋白身份：P00453
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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 |
|---|---|---|---|---|---|---|---|
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI 提交 1997-07-21 | Assembly 1 蛋白异源复合物 异源复合物；蛋白 × 3 PDB 声明：trimeric（3） 与蛋白数一致 |
链 D
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
链 P
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
|
未记录 | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 | X-RAY DIFFRACTION |
X-ray结晶条件
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
分辨率 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI 提交 1997-07-21 | Assembly 2 蛋白异源复合物 异源复合物；蛋白 × 2 PDB 声明：dimeric（2） 与蛋白数一致 |
链 E
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
|
未记录 | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 | X-RAY DIFFRACTION |
X-ray结晶条件
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
分辨率 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI 提交 1997-07-21 | Assembly 3 蛋白异源复合物 异源复合物；蛋白 × 2 PDB 声明：dimeric（2） 与蛋白数一致 |
链 F
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
|
未记录 | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 | X-RAY DIFFRACTION |
X-ray结晶条件
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
分辨率 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI 提交 1997-07-21 | Assembly 4 蛋白异源复合物 异源复合物；蛋白 × 15 PDB 声明：pentadecameric（15） 与蛋白数一致 |
链 D
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
链 E
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
链 P
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
|
未记录 | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 | X-RAY DIFFRACTION |
X-ray结晶条件
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
分辨率 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI 提交 1997-07-21 | Assembly 5 蛋白异源复合物 异源复合物；蛋白 × 12 PDB 声明：dodecameric（12） 与蛋白数一致 |
链 F
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
|
未记录 | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 | X-RAY DIFFRACTION |
X-ray结晶条件
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
分辨率 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI 提交 1997-07-21 | Assembly 6 蛋白异源复合物 异源复合物；蛋白 × 12 PDB 声明：dodecameric（12） 与蛋白数一致 |
链 D
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
链 E
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
|
未记录 | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 | X-RAY DIFFRACTION |
X-ray结晶条件
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
分辨率 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI 提交 1997-07-21 | Assembly 7 蛋白异源复合物 异源复合物；蛋白 × 9 PDB 声明：nonameric（9） 与蛋白数一致 |
链 P
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
|
未记录 | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 | X-RAY DIFFRACTION |
X-ray结晶条件
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
分辨率 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI 提交 1997-07-21 | Assembly 9 蛋白异源复合物 异源复合物；蛋白 × 2 PDB 声明：dimeric（2） 与蛋白数一致 |
链 D
356–375（20 aa）
片段：C-TERMINAL PORTION, 20 RESIDUES
|
未记录 | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 | X-RAY DIFFRACTION |
X-ray结晶条件
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
分辨率 3.00 Å R-free 0.287 |