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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：P0A731 New Search
5PDB entries
5Biological assembly
27chain/assembly records
Main Difference Dimensions in This Set
Different mutation/modification 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
1B93 METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI Deposited 1999-02-23 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–152（152 aa）
Chain B 1–152（152 aa）
Chain C 1–152（152 aa）
Not recorded FMT FORMIC ACID × 14 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 1.90 Å R-free 0.202
1EGH STRUCTURE OF METHYLGLYOXAL SYNTHASE COMPLEXED WITH THE COMPETITIVE INHIBITOR 2-PHOSPHOGLYCOLATE Deposited 2000-02-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–152（152 aa）
Chain B 1–152（152 aa）
Chain C 1–152（152 aa）
Chain D 1–152（152 aa）
Chain E 1–152（152 aa）
Chain F 1–152（152 aa）
Not recorded PGA 2-PHOSPHOGLYCOLIC ACID × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；PEG 1500, sodium cacodylate, imidazole-HCL, potassium phosphate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.00 Å R-free 0.219
1IK4 X-ray Structure of Methylglyoxal Synthase from E. coli Complexed with Phosphoglycolohydroxamic Acid Deposited 2001-05-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–152（152 aa）
Chain B 1–152（152 aa）
Chain C 1–152（152 aa）
Chain D 1–152（152 aa）
Chain E 1–152（152 aa）
Chain F 1–152（152 aa）
Not recorded PGH PHOSPHOGLYCOLOHYDROXAMIC ACID × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；PEG 1500, Sodium Cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.00 Å R-free 0.206
1S89 H98N Mutant of Methylglyoxal Synthase from E. coli complexed with Phosphoglycolic Acid Deposited 2004-01-31 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–152（152 aa）
Chain B 1–152（152 aa）
Chain C 1–152（152 aa）
Chain D 1–152（152 aa）
Chain E 1–152（152 aa）
Chain F 1–152（152 aa）
Mutation：H98N Mutation：H98N Mutation：H98N Mutation：H98N Mutation：H98N Mutation：H98N PGA 2-PHOSPHOGLYCOLIC ACID × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；298 K；PEG 1500, Sodium Cacodylate, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.22 Å R-free 0.229
1S8A H98Q Mutant of Methylglyoxal Synthase from E. coli complexed with Phosphoglycolic Acid Deposited 2004-01-31 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–152（152 aa）
Chain B 1–152（152 aa）
Chain C 1–152（152 aa）
Chain D 1–152（152 aa）
Chain E 1–152（152 aa）
Chain F 1–152（152 aa）
Mutation：H98Q Mutation：H98Q Mutation：H98Q Mutation：H98Q Mutation：H98Q Mutation：H98Q PGA 2-PHOSPHOGLYCOLIC ACID × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；PEG 1500, Sodium Cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.20 Å R-free 0.227

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.