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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：P27797 New Search
10PDB entries
14Biological assembly
37chain/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
2CLR THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE Deposited 1994-08-01 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 1–10（10 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
2CLR THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE Deposited 1994-08-01 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain F 1–10（10 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
3DOW Complex structure of GABA type A receptor associated protein and its binding epitope on calreticulin Deposited 2008-07-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 195–205（11 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；0.1 M MES, 27% v/v PEG MME 550, 10 mM ZnSO4, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K
Resolution 2.30 Å R-free 0.270
3POS Crystal structure of the globular domain of human calreticulin Deposited 2010-11-23 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 18–204（187 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG
Chain A 302–368（67 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.1 K；30% PEG 4000, 0.1M sodium acetate, 0.1M Tris, pH 8.5-9, VAPOR DIFFUSION, HANGING DROP, temperature 277.1K
Resolution 1.65 Å R-free 0.205
3POS Crystal structure of the globular domain of human calreticulin Deposited 2010-11-23 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 18–204（187 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG
Chain B 302–368（67 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.1 K；30% PEG 4000, 0.1M sodium acetate, 0.1M Tris, pH 8.5-9, VAPOR DIFFUSION, HANGING DROP, temperature 277.1K
Resolution 1.65 Å R-free 0.205
3POS Crystal structure of the globular domain of human calreticulin Deposited 2010-11-23 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 18–204（187 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG
Chain C 302–368（67 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.1 K；30% PEG 4000, 0.1M sodium acetate, 0.1M Tris, pH 8.5-9, VAPOR DIFFUSION, HANGING DROP, temperature 277.1K
Resolution 1.65 Å R-free 0.205
3POW Crystal structure of the globular domain of human calreticulin Deposited 2010-11-23 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 18–204（187 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG
Chain A 302–368（67 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6；277.1 K；30% PEG 4000, 0.2M ammonium acetate, 10mM magnesium acetate, and either 0.05M MES (pH 5.7 or 6.0), or 0.05M HEPES (pH 7.0), VAPOR DIFFUSION, temperature 277.1K
Resolution 1.55 Å R-free 0.191
5LK5 Crystal structure of the globular domain of human calreticulin mutant D71K Deposited 2016-07-21 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain A 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain B 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain B 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain C 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain C 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain D 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain D 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain E 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain E 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain F 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain F 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain G 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain G 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain H 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain H 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain I 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain I 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain J 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Chain J 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368
Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K CA CALCIUM ION × 10 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；30% PEG4000 0.2 M MgCl2 0.1 M Tris-HCl
Resolution 2.30 Å R-free 0.247
5V90 Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin Deposited 2017-03-22 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 238–273（36 aa） Fragment：UNP residues 238-273
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；2.0 M ammonium sulfate, 0.1 M HEPES pH 7.5
Resolution 3.25 Å R-free 0.262
5V90 Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin Deposited 2017-03-22 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 238–273（36 aa） Fragment：UNP residues 238-273
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；2.0 M ammonium sulfate, 0.1 M HEPES pH 7.5
Resolution 3.25 Å R-free 0.262
6ENY Structure of the human PLC editing module Deposited 2017-10-07 Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain G 18–417（400 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.80 Å
7QPD Structure of the human MHC I peptide-loading complex editing module Deposited 2022-01-03 Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 18–417（400 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.73 Å
8TZO Structure of human Wnt7a bound to WLS and CALR Deposited 2023-08-27 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 1–417（417 aa）
Not recorded PAM PALMITOLEIC ACID × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
8TZR Structure of human Wnt3a bound to WLS and CALR Deposited 2023-08-27 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 1–417（417 aa）
Not recorded PAM PALMITOLEIC ACID × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 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.