当前蛋白身份:P06278 重新检索
本组结构的主要差异维度
构建体不同 突变/修饰不同 组装状态不同 配体/离子不同 实验环境不同 结构质量指标不同

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
1BLI BACILLUS LICHENIFORMIS ALPHA-AMYLASE 提交 1998-01-07 Assembly 1 蛋白单体 单体;蛋白 × 1 PDB 声明:monomeric(1) 与蛋白数一致
链 A 30–512(483 aa)
突变:N190F, Q264S, N265Y CA CALCIUM ION × 3 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray结晶条件 pH 7;pH 7.0
分辨率 1.90 Å R-free 0.185
1BPL GLYCOSYLTRANSFERASE 提交 1995-07-13 Assembly 1 蛋白同源多聚体 同源多聚体;蛋白 × 2 PDB 声明:dimeric(2) 与蛋白数一致
链 A 30–218(189 aa)
链 B 219–512(294 aa)
未记录 未记录非水小分子 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION;pH 8.2;MOLECULE: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE FROM BACILLUS LICHENIFORMIS. VAPOR DIFFUSION, ROOM TEMPERATURE PROTEIN SOLUTION: 15 MG/ML BLA IN 0.4 M SODIUM CITRATE 2.5 MM EDTA, PH 8.2 RESERVOIR: 0.66 M SODIUM CITRATE, 2.5 MM EDTA, PH 8.2 CALCIUM REMOVAL BY EDTA LEADS TO A CLEAVAGE OF BLA AFTER GLU 189 DUE TO TRACE AMOUNTS OF A GLU-C-ENDOPEPTIDASE PRESENT IN THE PREPARATION (SEE PAPER)., vapor diffusion
分辨率 2.20 Å
1E3X Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A 提交 2000-06-26 Assembly 1 信息不足 单体;蛋白 × 1 PDB 声明:monomeric(1) 与蛋白数一致
链 A 330–512(183 aa)
未记录 CA CALCIUM ION × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML.
分辨率 1.90 Å R-free 0.200
1E3Z Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A 提交 2000-06-27 Assembly 1 信息不足 单体;蛋白 × 1 PDB 声明:monomeric(1) 与蛋白数一致
链 A 330–512(183 aa)
未记录 CA CALCIUM ION × 4 NA SODIUM ION × 1 ACI 6-AMINO-4-HYDROXYMETHYL-CYCLOHEX-4-ENE-1,2,3-TRIOL × 3 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML. CRYSTALS WERE THEN SOAKED IN 10MM ACARBOSE SOLUTION TO OBTAIN THE COMPLEX.
分辨率 1.93 Å R-free 0.200
1E40 Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A 提交 2000-06-27 Assembly 1 信息不足 单体;蛋白 × 1 PDB 声明:monomeric(1) 与蛋白数一致
链 A 330–512(183 aa)
未记录 CA CALCIUM ION × 4 NA SODIUM ION × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML. CRYSTALS WERE THEN SOAKED IN 10MM MALTOTRIOSE SOLUTION TO OBTAIN THE COMPLEX.
分辨率 2.20 Å R-free 0.210
1E43 Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A 提交 2000-06-27 Assembly 1 信息不足 单体;蛋白 × 1 PDB 声明:monomeric(1) 与蛋白数一致
链 A 330–512(183 aa)
未记录 CA CALCIUM ION × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP;pH 10;291 K;CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML.
分辨率 1.70 Å R-free 0.185
1OB0 Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface 提交 2003-01-21 Assembly 1 蛋白单体 单体;蛋白 × 1 PDB 声明:monomeric(1) 与蛋白数一致
链 A 30–512(483 aa)
突变:YES CA CALCIUM ION × 3 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray结晶条件 VAPOR DIFFUSION;pH 7;PROTEIN WAS CRYSTALLIZED BY VAPOR DIFFUSION FROM DROPS CONTAINING 4 UL OF PROTEIN SOLUTION (10 MG/ML IN 50 MM TRIS/HCL, PH 8.0) PLUS 4 UL OF RESERVOIR SOLUTION (50 MM HEPES, 1 M AMMONIUM SULFATE, 1% (V/V) PEG 500, PH 7.0) EQUILIBRATED AGAINST 1 ML OF RESERVOIR SOLUTION.
分辨率 1.83 Å R-free 0.154
1VJS STRUCTURE OF ALPHA-AMYLASE PRECURSOR 提交 1996-10-02 Assembly 1 蛋白单体 单体;蛋白 × 1 PDB 声明:monomeric(1) 与蛋白数一致
链 A 30–512(483 aa)
未记录 未记录非水小分子 X-RAY DIFFRACTION mmCIF 未提供已读取条件 分辨率 1.70 Å R-free 0.226