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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：P19883 New Search
4PDB entries
4Biological assembly
8chain/assembly records
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
2B0U The Structure of the Follistatin:Activin Complex Deposited 2005-09-14 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 30–317（288 aa） Fragment：Follistatin-288
Chain D 30–317（288 aa） Fragment：Follistatin-288
Not recorded IR3 IRIDIUM (III) ION × 5 MLI MALONATE ION × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；PEG 3350, 200 mM Malonate, pH 7.0, vapor diffusion, hanging drop, temperature 295K
Resolution 2.80 Å R-free 0.297
2P6A The structure of the Activin:Follistatin 315 complex Deposited 2007-03-16 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 30–344（315 aa）
Chain D 30–344（315 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；20-23% PEG 1000, 200mM MgCl2, 3% EtOH, 20mM Trimethyl-amine HCl, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298 K
Resolution 3.40 Å R-free 0.324
3HH2 Crystal structure of the myostatin:follistatin 288 complex Deposited 2009-05-14 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 30–317（288 aa） Fragment：UNP residues 30-317
Chain D 30–317（288 aa） Fragment：UNP residues 30-317
Not recorded PO4 PHOSPHATE ION × 3 CIT CITRIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；PEG 1000, Ethanol, Phosphate/citrate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.15 Å R-free 0.249
5JHW Crystal Structure of the GDF11:Follistatin 288 complex Deposited 2016-04-21 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 30–317（288 aa） Fragment：UNP residues 30-317
Chain D 30–317（288 aa） Fragment：UNP residues 30-317
Not recorded PO4 PHOSPHATE ION × 3 FLC CITRATE ANION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；298 K；100mM Phosphate/Citrate pH 4.2, 14% EtOH, 1% PEG 1000
Resolution 2.35 Å R-free 0.247

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.