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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P0A759 New Search
10PDB entries
14Biological assembly
19chain/assembly records
Main Difference Dimensions in This Set
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
1CD5 GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER Deposited 1999-03-05 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7；293 K；sodium acetate, hepes, pH 7.0, VAPOR DIFFUSION, temperature 293K
Resolution 2.30 Å R-free 0.252
1DEA STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION Deposited 1995-09-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Chain B 1–266（266 aa）
Not recorded PO4 PHOSPHATE ION × 12 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å
1DEA STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION Deposited 1995-09-13 Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–266（266 aa）
Not recorded PO4 PHOSPHATE ION × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å
1DEA STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION Deposited 1995-09-13 Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 1–266（266 aa）
Not recorded PO4 PHOSPHATE ION × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å
1FQO GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE SUBSTRATE OF THE REVERSE REACTION FRUCTOSE 6-PHOSPHATE (OPEN FORM) Deposited 2000-09-06 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Chain B 1–266（266 aa）
Not recorded F6R FRUCTOSE -6-PHOSPHATE × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；sodium acetate, HEPES, fructose 6-phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP at 291K
Resolution 2.20 Å R-free 0.233
1FRZ GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, R CONFORMER. COMPLEXED WITH THE ALLOSTERIC ACTIVATOR N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AT 2.2 A RESOLUTION Deposited 2000-09-07 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Chain B 1–266（266 aa）
Not recorded 16G 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；HEPES, sodium acetate, pH 7.5, VAPOR DIFFUSION, HANGING DROP at 291K
Resolution 2.20 Å R-free 0.227
1FS5 A DISCOVERY OF THREE ALTERNATE CONFORMATIONS IN THE ACTIVE SITE OF GLUCOSAMINE-6-PHOSPHATE ISOMERASE Deposited 2000-09-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Chain B 1–266（266 aa）
Not recorded 16G 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose × 6 TLA L(+)-TARTARIC ACID × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；HEPES, sodium potassium tatrate, pH 7.0, VAPOR DIFFUSION, HANGING DROP at 291K
Resolution 1.73 Å R-free 0.251
1FS6 GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER, AT 2.2A RESOLUTION Deposited 2000-09-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；291 K；HEPES, sodium acetate, pH 6.8, VAPOR DIFFUSION, HANGING DROP at 291K
Resolution 2.20 Å R-free 0.235
1FSF GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER, AT 1.9A RESOLUTION Deposited 2000-09-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；291 K；HEPES, sodium acetate, pH 6.8, VAPOR DIFFUSION, HANGING DROP at 291K
Resolution 1.90 Å R-free 0.232
1HOR STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION Deposited 1995-09-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Chain B 1–266（266 aa）
Not recorded PO4 PHOSPHATE ION × 6 AGP 2-DEOXY-2-AMINO GLUCITOL-6-PHOSPHATE × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.40 Å
1JT9 Structure of the mutant F174A T form of the Glucosamine-6-Phosphate deaminase from E.coli Deposited 2001-08-20 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–266（266 aa）
Mutation：F174A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；HEPES, sodium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.06 Å R-free 0.224
1JT9 Structure of the mutant F174A T form of the Glucosamine-6-Phosphate deaminase from E.coli Deposited 2001-08-20 Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–266（266 aa）
Mutation：F174A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；HEPES, sodium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.06 Å R-free 0.224
2WU1 Glucosamine-6-Phosphate Deaminase Complexed with the Allosteric Activator N-Acetyl-Glucoamine-6-Phosphate both in the Active and Allosteric sites. Deposited 2009-09-25 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–266（266 aa）
Not recorded 16G 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose × 1 FGS 5-(ACETYLAMINO)-5-DEOXY-1-O-PHOSPHONO-L-IDITOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；SODIUM ACETATE, HEPES, N-ACETYL-GLUCOSAMINE-6-PHOSPHATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP AT 291K
Resolution 2.20 Å R-free 0.191
2WU1 Glucosamine-6-Phosphate Deaminase Complexed with the Allosteric Activator N-Acetyl-Glucoamine-6-Phosphate both in the Active and Allosteric sites. Deposited 2009-09-25 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 1–266（266 aa）
Not recorded 16G 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose × 1 FGS 5-(ACETYLAMINO)-5-DEOXY-1-O-PHOSPHONO-L-IDITOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；SODIUM ACETATE, HEPES, N-ACETYL-GLUCOSAMINE-6-PHOSPHATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP AT 291K
Resolution 2.20 Å R-free 0.191

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.