Current Protein Identity:P00725 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
1CEL THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI Deposited 1994-05-17 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 19–451(433 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 BGC beta-D-glucopyranose × 1 CA CALCIUM ION × 1 IBZ 2-IODOBENZYLTHIO GROUP × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å
1CEL THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI Deposited 1994-05-17 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 19–451(433 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 IBZ 2-IODOBENZYLTHIO GROUP × 1 GLC alpha-D-glucopyranose × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å
1Q2E CELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245-252 AND BOUND NON-HYDROLYSABLE CELLOTETRAOSE Deposited 2003-07-24 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 18–451(434 aa) Fragment:CATALYTIC DOMAIN 1-434
Mutation:245-252 DELETION Non-standard monomer:Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG 5000, TRIS-HCL, ETHYLENE GLYCOL, CALCIUM CHLORIDE, SODIUM ACETATE, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.75 Å R-free 0.239
1Q2E CELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245-252 AND BOUND NON-HYDROLYSABLE CELLOTETRAOSE Deposited 2003-07-24 Assembly 2 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 18–451(434 aa) Fragment:CATALYTIC DOMAIN 1-434
Mutation:245-252 DELETION Non-standard monomer:Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG 5000, TRIS-HCL, ETHYLENE GLYCOL, CALCIUM CHLORIDE, SODIUM ACETATE, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.75 Å R-free 0.239
3CEL ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH CELLOBIOSE BOUND IN THE ACTIVE SITE Deposited 1996-08-24 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 19–451(433 aa) Fragment:CATALYTIC DOMAIN, RESIDUES 1 - 434
Mutation:E212Q Non-standard monomer:Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CD CADMIUM ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6;50 MM MES PH 6.0, 5% MONOMETHYL ETHER PEG 5000, 5 MM CDCL2, 1 MM CELLOBIOSE
Resolution 2.00 Å R-free 0.256
5CEL CBH1 (E212Q) CELLOTETRAOSE COMPLEX Deposited 1997-09-24 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 19–451(433 aa) Fragment:CATALYTIC DOMAIN, RESIDUES 1 - 434
Mutation:E212Q Non-standard monomer:Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6;HANGING DROPS. EQUAL VOLUMES OF 8 MG/ML PROTEIN AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 6.0), 18% (W/V) MONOMETHYLETHER PEG 5000, 0.01 M COCL2, AND 0.02% NA-AZIDE. CRYOPROTECTANT/SOAK SOLUTION CONTAINED 0.1 M MES (PH 6.0), 20% (W/V) MONOMETHYLETHER PEG 5000, 0.01 M COCL2, 20% GLYCEROL AND 0.005 M CELLOTETRAOSE. THE AXES OF THE CRYO-COOLED CRYSTALS ARE SYSTEMATICALLY SHORTER THAN THOSE OF CRYSTALS COLLECTED AT ROOM TEMPERATURE. IN ORDER TO KEEP THE SAME INDEXING AS IN PREVIOUS ROOM-TEMPERATURE DATA SETS, THE LONGER A-AXIS IS LISTED BEFORE THE SHORTER B-AXIS., vapor diffusion - hanging drop
Resolution 1.90 Å R-free 0.240
6CEL CBH1 (E212Q) CELLOPENTAOSE COMPLEX Deposited 1997-09-24 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 19–451(433 aa) Fragment:CATALYTIC DOMAIN, RESIDUES 1 - 434
Mutation:E212Q Non-standard monomer:Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CO COBALT (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6;HANGING DROPS. EQUAL VOLUMES OF 8 MG/ML PROTEIN AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 6.0), 18% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, AND 0.02% NA-AZIDE. CRYOPROTECTANT/SOAK SOLUTION CONTAINED 0.1 M MES (PH 6.0), 20% (W/V) MONOMETHYLETHER PEG 5000, 0.01 M COCL2, 15% GLYCEROL AND 0.004 M CELLOTETRAOSE. THE AXES OF THE CRYO-COOLED CRYSTALS ARE SYSTEMATICALLY SHORTER THAN THOSE OF CRYSTALS COLLECTED AT ROOM TEMPERATURE. IN ORDER TO KEEP THE SAME INDEXING AS IN PREVIOUS ROOM-TEMPERATURE DATA SETS, THE LONGER A-AXIS IS LISTED BEFORE THE SHORTER B-AXIS., vapor diffusion - hanging drop
Resolution 1.70 Å R-free 0.235
7CEL CBH1 (E217Q) IN COMPLEX WITH CELLOHEXAOSE AND CELLOBIOSE Deposited 1997-09-24 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 19–451(433 aa) Fragment:CATALYTIC DOMAIN, RESIDUES 1 - 434
Mutation:E217Q Non-standard monomer:Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6;HANGING DROPS. EQUAL VOLUMES OF 8 MG/ML PROTEIN AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 6.0), 18% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, AND 0.02% NA-AZIDE., vapor diffusion - hanging drop
Resolution 1.90 Å R-free 0.215