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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：P20065 New Search
2PDB entries
2Biological assembly
2chain/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
1T44 Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation Deposited 2004-04-28 Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 28–46（19 aa） Fragment：Chimera of Gelsolin domain 1 (residues 28-152) from human and C-Terminal domain of thymosin Beta-4 from mouse (residues 153-171)
Not recorded CA CALCIUM ION × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 6.5；293 K；PEG 8000, Sodium acetate, calcium chloride, pH 6.5, microbatch, temperature 293K
Resolution 2.00 Å R-free 0.195
3M3N Structure of a Longitudinal Actin Dimer Assembled by Tandem W Domains Deposited 2010-03-09 Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain W 26–50（25 aa） Fragment：Engineered tandem W domain construct 3W
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；300 K；100 mM CAPS pH 10.0, and 24% PEG 3350, 100 mM RbCl, VAPOR DIFFUSION, HANGING DROP, temperature 300.0K
Resolution 7.00 Å

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.