Current Protein Identity:P16098 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental conditions Different structure-quality metrics

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
1B1Y SEVENFOLD MUTANT OF BARLEY BETA-AMYLASE Deposited 1998-11-25 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 5–504(500 aa)
Mutation:M185L,S295A,I297V,S350P,S351P,Q352D,A376S BGC beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.1;HUNGING DROP VAPOR DIFFUSION AGAINST 0.1 M PIPES PH 7.1, 0.1 M MGAC2 AND 14% PEG 6000 WITH A PROTEIN CONCENTRATION OF 3 MG/ML., vapor diffusion - hanging drop
Resolution 2.50 Å R-free 0.256
2XFF Crystal structure of Barley Beta-Amylase complexed with acarbose Deposited 2010-05-28 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–535(535 aa)
Not recorded EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;CRYSTALS WERE GROWN AT 291 K USING THE HANGING DROP VAPOUR DIFFUSION METHOD WITH PROTEIN AT 10 MG PER ML AND A PRECIPITANT COMPRISED OF 14 PERCENT PEG 3350 IN 100 MM BIS-TRIS PROPANE BUFFER AT PH 5.5
Resolution 1.31 Å R-free 0.155
2XFR Crystal structure of barley beta-amylase at atomic resolution Deposited 2010-05-28 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–535(535 aa)
Not recorded EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;CRYSTALS WERE GROWN AT 291 K USING THE HANGING DROP VAPOUR DIFFUSION METHOD WITH PROTEIN AT 10 MG PER ML AND A PRECIPITANT COMPRISED OF 14 PERCENT PEG 3350 IN 100 MM BIS-TRIS PROPANE BUFFER AT PH 5.5
Resolution 0.97 Å R-free 0.130
2XFY Crystal structure of Barley Beta-Amylase complexed with alpha- cyclodextrin Deposited 2010-05-28 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–535(535 aa)
Not recorded EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;CRYSTALS WERE GROWN AT 291 K USING THE HANGING DROP VAPOUR DIFFUSION METHOD WITH PROTEIN AT 10 MG PER ML AND A PRECIPITANT COMPRISED OF 14 PERCENT PEG 3350 IN 100 MM BIS-TRIS PROPANE BUFFER AT PH 5.5
Resolution 1.21 Å R-free 0.153
2XG9 Crystal structure of Barley Beta-Amylase complexed with 4-O-alpha-D- glucopyranosylmoranoline Deposited 2010-06-02 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–535(535 aa)
Not recorded EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;CRYSTALS WERE GROWN AT 291 K USING THE HANGING DROP VAPOUR DIFFUSION METHOD WITH PROTEIN AT 10 MG PER ML AND A PRECIPITANT COMPRISED OF 14 PERCENT PEG 3350 IN 100 MM BIS-TRIS PROPANE BUFFER AT PH 5.5
Resolution 1.80 Å R-free 0.171
2XGB Crystal structure of Barley Beta-Amylase complexed with 2,3- epoxypropyl-alpha-D-glucopyranoside Deposited 2010-06-02 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–535(535 aa)
Not recorded EPG (2R)-oxiran-2-ylmethyl alpha-D-glucopyranoside × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;CRYSTALS WERE GROWN AT 291 K USING THE HANGING DROP VAPOUR DIFFUSION METHOD WITH PROTEIN AT 10 MG PER ML AND A PRECIPITANT COMPRISED OF 14 PERCENT PEG 3350 IN 100 MM BIS-TRIS PROPANE BUFFER AT PH 5.5
Resolution 1.20 Å R-free 0.141
2XGI Crystal structure of Barley Beta-Amylase complexed with 3,4- epoxybutyl alpha-D-glucopyranoside Deposited 2010-06-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–535(535 aa)
Not recorded EDO 1,2-ETHANEDIOL × 2 J5B (3R)-3-hydroxybutyl alpha-D-glucopyranoside × 1 EBQ (3S)-3-hydroxybutyl alpha-D-glucopyranoside × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;CRYSTALS WERE GROWN AT 291 K USING THE HANGING DROP VAPOUR DIFFUSION METHOD WITH PROTEIN AT 10 MG PER ML AND A PRECIPITANT COMPRISED OF 14 PERCENT PEG 3350 IN 100 MM BIS-TRIS PROPANE BUFFER AT PH 5.5
Resolution 1.30 Å R-free 0.158