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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：P0AC86 New Search
8PDB entries
10Biological assembly
32chain/assembly records
Main Difference Dimensions in This Set
Different mutation/modification Different assembly state Different ligand/ion Different experimental method 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
9S7V Structure of glycogen phosphorylase - dimeric form - from Escherichia coli Deposited 2025-08-05 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9S86 Structure of glycogen phosphorylase - tetrameric form - from Escherichia coli Deposited 2025-08-05 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Chain C 1–815（815 aa）
Chain D 1–815（815 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.97 Å
9S8B Structure of glycogen phosphorylase - dimeric form - in complex with HPr from Escherichia coli Deposited 2025-08-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.79 Å
9S8K Structure of glycogen phosphorylase - tetrameric form - in complex with HPr from Escherichia coli Deposited 2025-08-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Chain C 1–815（815 aa）
Chain D 1–815（815 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.06 Å
9UKQ Crystal structure of glycogen phosphorylase from Escherichia coli Deposited 2025-04-18 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Chain C 1–815（815 aa）
Chain D 1–815（815 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；Protein conc: 10.4mg/mL; 0.1M MES pH 6.0, 9% (v/v) PEG 3350
Resolution 3.50 Å R-free 0.273
9UKQ Crystal structure of glycogen phosphorylase from Escherichia coli Deposited 2025-04-18 Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain E 1–815（815 aa）
Chain F 1–815（815 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；Protein conc: 10.4mg/mL; 0.1M MES pH 6.0, 9% (v/v) PEG 3350
Resolution 3.50 Å R-free 0.273
9UKR Crystal structure of glycogen phosphorylase from E. coli in complex with AMP Deposited 2025-04-18 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Chain C 1–815（815 aa）
Chain D 1–815（815 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) AMP ADENOSINE MONOPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；Protein conc: 10.4mg/mL; Reservoir: 0.1M MES pH 6.0, 9% (v/v) PEG 3350
Resolution 3.55 Å R-free 0.272
9UKR Crystal structure of glycogen phosphorylase from E. coli in complex with AMP Deposited 2025-04-18 Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain E 1–815（815 aa）
Chain F 1–815（815 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) AMP ADENOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；Protein conc: 10.4mg/mL; Reservoir: 0.1M MES pH 6.0, 9% (v/v) PEG 3350
Resolution 3.55 Å R-free 0.272
9V16 Crystal structure of E. coli glycogen phosphorylase N185A/R267E mutant in complex with AMP Deposited 2025-05-19 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Chain C 1–815（815 aa）
Chain D 1–815（815 aa）
Mutation：N185A/R267E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N185A/R267E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N185A/R267E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N185A/R267E Non-standard monomer：Yes (specific site not provided by mmCIF) AMP ADENOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2% v/v 1,4-dioxane, 0.1M Tris pH 8.0, 15% w/v polyethylene glycol 3350 (The crystal was soaked in a solution supplemented with 40 mM AMP before data collection)
Resolution 3.45 Å R-free 0.235
9V17 Crystal structure of E. coli glycogen phosphorylase N185A/R267E mutant Deposited 2025-05-19 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–815（815 aa）
Chain B 1–815（815 aa）
Chain C 1–815（815 aa）
Chain D 1–815（815 aa）
Mutation：N185A/R267E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N185A/R267E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N185A/R267E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N185A/R267E Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2% v/v 1,4-dioxane, 0.1M Tris pH 8.0, 15% w/v polyethylene glycol 3350
Resolution 3.70 Å R-free 0.229

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.