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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：P35221 New Search
9PDB entries
13Biological assembly
21chain/assembly records
Main Difference Dimensions in This Set
Different construct 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
1H6G alpha-catenin M-domain Deposited 2001-06-14 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 377–632（256 aa） Fragment：M-FRAGMENT, RESIDUES 377-632
Non-standard monomer：Yes (specific site not provided by mmCIF) MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.6；30 % (V/V) MPD, 0.1 M SODIUM ACETETE BUFFER, PH 4.6, 20 MM CALCIUM CHLORIDE
Resolution 2.20 Å R-free 0.257
1H6G alpha-catenin M-domain Deposited 2001-06-14 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 377–632（256 aa） Fragment：M-FRAGMENT, RESIDUES 377-632
Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.6；30 % (V/V) MPD, 0.1 M SODIUM ACETETE BUFFER, PH 4.6, 20 MM CALCIUM CHLORIDE
Resolution 2.20 Å R-free 0.257
1L7C alpha-catenin fragment, residues 385-651 Deposited 2002-03-14 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 385–651（267 aa） Fragment：Residues 385-651
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, HANGING DROP；pH 4；293 K；sodium acetate, dithiothreitol, urea, sodium/potassium tartrate, isopropanol, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.273
1L7C alpha-catenin fragment, residues 385-651 Deposited 2002-03-14 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 385–651（267 aa） Fragment：Residues 385-651
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, HANGING DROP；pH 4；293 K；sodium acetate, dithiothreitol, urea, sodium/potassium tartrate, isopropanol, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.273
1L7C alpha-catenin fragment, residues 385-651 Deposited 2002-03-14 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 385–651（267 aa） Fragment：Residues 385-651
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, HANGING DROP；pH 4；293 K；sodium acetate, dithiothreitol, urea, sodium/potassium tartrate, isopropanol, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.273
1L7C alpha-catenin fragment, residues 385-651 Deposited 2002-03-14 Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 385–651（267 aa） Fragment：Residues 385-651
Chain C 385–651（267 aa） Fragment：Residues 385-651
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, HANGING DROP；pH 4；293 K；sodium acetate, dithiothreitol, urea, sodium/potassium tartrate, isopropanol, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.273
4EHP Crystal Structure of human vinculin head domain (residues 1-252) in complex with alpha-catenin (residues 277-382) Deposited 2012-04-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 277–382（106 aa） Fragment：unp residues 277-382
Not recorded ACT ACETATE ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；295 K；PEG 3350, sodium acetate, VAPOR DIFFUSION, temperature 295K
Resolution 2.66 Å R-free 0.229
4IGG Full-length human alpha-catenin crystal structure Deposited 2012-12-17 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 82–906（825 aa） Fragment：UNP residues 82-906
Chain B 82–906（825 aa） Fragment：UNP residues 82-906
Not recorded PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.8；295 K；0.9 M Na/K Phosphate, 0.3 M Na Malonate, pH 6.8, VAPOR DIFFUSION, temperature 295K
Resolution 3.66 Å R-free 0.241
6UPV Alpha-E-catenin ABD-F-actin complex Deposited 2019-10-18 Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric（7） Consistent with protein count
Chain L 1–906（906 aa）
Chain M 1–906（906 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
7UTJ Cryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin Deposited 2022-04-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric（12） Consistent with protein count
Chain G 22–906（885 aa）
Chain H 22–906（885 aa）
Chain I 22–906（885 aa）
Chain K 22–906（885 aa）
Chain L 22–906（885 aa）
Chain Z 22–906（885 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.77 Å
9BL2 KIR3DL1*001 in complex with HLA-B*57:03 presenting the AW10 peptide Deposited 2024-04-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 850–859（10 aa） Fragment：residues 850-859 (Uniprot numbering)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；294 K；18% PEG-3350, 2% tacsimate pH 5.0, 0.1 M tri-sodium citrate pH 5.6
Resolution 2.10 Å R-free 0.231
9BL3 KIR3DL1*114 in complex with HLA-B*57:03 presenting the AW10 peptide Deposited 2024-04-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 850–859（10 aa） Fragment：residues 850-859 (Uniprot numbering)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；294 K；16% PEG 3350, 2% tacsimate pH 5.0, 0.1 M tri-sodium citrate pH 5.6
Resolution 2.00 Å R-free 0.229
9BL4 KIR3DL1*086 in complex with HLA-B*57:03 presenting the AW10 peptide Deposited 2024-04-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 850–859（10 aa） Fragment：residues 850-859 (Uniprot numbering)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；294 K；16% PEG 3350, 2% tacsimate pH 5.0, 0.1 M tri-sodium citrate pH 5.6
Resolution 1.75 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.