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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：K4FZF8 New Search
6PDB entries
7Biological assembly
20chain/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
10NM CRYO-EM STRUCTURE OF THE A149T DIMER VARIANT OF SERINE HYDROXYMETHYLTRANSFERASE 8 FROM SOYBEAN CULTIVAR ESSEX IN COMPLEX WITH PLP Deposited 2026-01-28 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–471（471 aa）
Chain B 1–471（471 aa）
Mutation：A149T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A149T Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；50mM HEPES, 150mM NaCl, 0.5mM TCEP
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.92 Å
6UXH Structure of serine hydroxymethyltransferase 8 from Glycine max cultivar Essex complexed with PLP Deposited 2019-11-07 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–471（471 aa）
Chain B 1–471（471 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.175 M trimethylamine N-oxide, 0.1 M Tris (pH 8.5), 19.5% (w/v) PEG MME 2000
Resolution 1.86 Å R-free 0.231
6UXI Structure of serine hydroxymethyltransferase 8 from Glycine max cultivar Essex complexed with PLP-Glycine Deposited 2019-11-07 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–471（471 aa）
Chain B 1–471（471 aa）
Not recorded PLG N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE] × 4 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.19 M trimethylamine N-oxide, 0.1 M Tris (pH 8.5), 21% (w/v) PEG MME 2000, 20 mM glycine
Resolution 2.10 Å R-free 0.223
6UXJ Structure of serine hydroxymethyltransferase 8 from Glycine max cultivar Essex complexed with PLP-glycine and 5-formyltetrahydrofolate Deposited 2019-11-07 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–471（471 aa）
Chain B 1–471（471 aa）
Chain C 1–471（471 aa）
Chain D 1–471（471 aa）
Not recorded PLG N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE] × 4 FFO N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid × 4 EDO 1,2-ETHANEDIOL × 17 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.24 M trimethylamine N-oxide, 0.1 M Tris (pH 8.5), 20% (w/v) PEG MME 2000, 10 mM 5-formyl tetrahydrofolate, 20 mM glycine
Resolution 1.40 Å R-free 0.194
9Y6B CRYSTAL STRUCTURE OF A149T VARIANT OF SERINE HYDROXYMETHYLTRANSFERASE 8 FROM SOYBEAN CULTIVAR ESSEX IN COMPLEX WITH PLP-GLYCINE Deposited 2025-09-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–471（471 aa）
Chain B 1–471（471 aa）
Chain C 1–471（471 aa）
Chain D 1–471（471 aa）
Mutation：A149T Mutation：A149T Mutation：A149T Mutation：A149T PLG N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE] × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Ammonium phosphate dibasic 20% w/v Polyethylene glycol 3,350
Resolution 1.90 Å R-free 0.319
9YBZ CRYSTAL STRUCTURE OF THE A149T VARIANT OF SERINE HYDROXYMETHYLTRANSFERASE 8 FROM SOYBEAN CULTIVAR ESSEX IN COMPLEX WITH PLP Deposited 2025-09-17 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–471（471 aa）
Chain B 1–471（471 aa）
Chain C 1–471（471 aa）
Chain D 1–471（471 aa）
Mutation：A149T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A149T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A149T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A149T 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；0.1 M Ammonium tartrate dibasic pH 7.0 12% w/v Polyethylene glycol 3,350
Resolution 2.28 Å R-free 0.313
9YBZ CRYSTAL STRUCTURE OF THE A149T VARIANT OF SERINE HYDROXYMETHYLTRANSFERASE 8 FROM SOYBEAN CULTIVAR ESSEX IN COMPLEX WITH PLP Deposited 2025-09-17 Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain E 1–471（471 aa）
Chain F 1–471（471 aa）
Mutation：A149T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：A149T 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；0.1 M Ammonium tartrate dibasic pH 7.0 12% w/v Polyethylene glycol 3,350
Resolution 2.28 Å R-free 0.313

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.