Current Protein Identity：P06278
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1BLI BACILLUS LICHENIFORMIS ALPHA-AMYLASE Deposited 1998-01-07 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
30–512（483 aa）
|
Mutation：N190F, Q264S, N265Y | CA CALCIUM ION × 3 NA SODIUM ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 7；pH 7.0
|
Resolution 1.90 Å R-free 0.185 |
| 1BPL GLYCOSYLTRANSFERASE Deposited 1995-07-13 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
30–218（189 aa）
Chain B
219–512（294 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
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
|
Resolution 2.20 Å |
| 1E3X Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A Deposited 2000-06-26 | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
330–512（183 aa）
|
Not recorded | CA CALCIUM ION × 4 NA SODIUM ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
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.
|
Resolution 1.90 Å R-free 0.200 |
| 1E3Z Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A Deposited 2000-06-27 | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
330–512（183 aa）
|
Not recorded | 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 crystallization conditions
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.
|
Resolution 1.93 Å R-free 0.200 |
| 1E40 Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A Deposited 2000-06-27 | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
330–512（183 aa）
|
Not recorded | CA CALCIUM ION × 4 NA SODIUM ION × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
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.
|
Resolution 2.20 Å R-free 0.210 |
| 1E43 Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A Deposited 2000-06-27 | Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
330–512（183 aa）
|
Not recorded | CA CALCIUM ION × 4 NA SODIUM ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
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.
|
Resolution 1.70 Å R-free 0.185 |
| 1OB0 Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface Deposited 2003-01-21 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
30–512（483 aa）
|
Mutation：YES | CA CALCIUM ION × 3 NA SODIUM ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
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.
|
Resolution 1.83 Å R-free 0.154 |
| 1VJS STRUCTURE OF ALPHA-AMYLASE PRECURSOR Deposited 1996-10-02 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
30–512（483 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 1.70 Å R-free 0.226 |