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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：Q16655 New Search
16PDB entries
25Biological assembly
25chain/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
2GT9 Human Class I MHC HLA-A2 in complex with the decameric Melan-A/MART-1(26-35) peptide Deposited 2006-04-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 26–35（10 aa）
Not recorded GOL GLYCEROL × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；PEG3350 24%, MES 0.025M, NaCl 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.75 Å R-free 0.213
2GT9 Human Class I MHC HLA-A2 in complex with the decameric Melan-A/MART-1(26-35) peptide Deposited 2006-04-27 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain F 26–35（10 aa）
Not recorded GOL GLYCEROL × 3 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；PEG3350 24%, MES 0.025M, NaCl 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.75 Å R-free 0.213
2GTW Human Class I MHC HLA-A2 in complex with the nonameric Melan-A/MART-1(27-35) peptide having A27L substitution Deposited 2006-04-28 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 28–35（8 aa） Fragment：residues 27-35
Mutation：A27L GOL GLYCEROL × 3 FMT FORMIC ACID × 3 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；PEG 3350 24%, MES 0.025M, HCOOK 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.55 Å R-free 0.218
2GTW Human Class I MHC HLA-A2 in complex with the nonameric Melan-A/MART-1(27-35) peptide having A27L substitution Deposited 2006-04-28 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain F 28–35（8 aa） Fragment：residues 27-35
Mutation：A27L GOL GLYCEROL × 2 FMT FORMIC ACID × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；PEG 3350 24%, MES 0.025M, HCOOK 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.55 Å R-free 0.218
2GTZ Human Class I MHC HLA-A2 in complex with the nonameric Melan-A/MART-1(27-35) peptide having A28L substitution Deposited 2006-04-28 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 28–36（9 aa） Fragment：residues 27-35
Mutation：A28L GOL GLYCEROL × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；PEG 3350 24%, MES 0.025M, NH4Cl 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.70 Å R-free 0.217
2GTZ Human Class I MHC HLA-A2 in complex with the nonameric Melan-A/MART-1(27-35) peptide having A28L substitution Deposited 2006-04-28 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain F 28–36（9 aa） Fragment：residues 27-35
Mutation：A28L GOL GLYCEROL × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；PEG 3350 24%, MES 0.025M, NH4Cl 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.70 Å R-free 0.217
2GUO Human Class I MHC HLA-A2 in complex with the native nonameric Melan-A/MART-1(27-35) peptide Deposited 2006-05-01 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 27–35（9 aa）
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；PEG3350 24%, MES 0.025M, NaCl 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.90 Å R-free 0.244
2GUO Human Class I MHC HLA-A2 in complex with the native nonameric Melan-A/MART-1(27-35) peptide Deposited 2006-05-01 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain F 27–35（9 aa）
Not recorded GOL GLYCEROL × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；PEG3350 24%, MES 0.025M, NaCl 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.90 Å R-free 0.244
3L6F Structure of MHC class II molecule HLA-DR1 complexed with phosphopeptide MART-1 Deposited 2009-12-23 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 100–114（15 aa） Fragment：UNP residues 100-114
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.5；298 K；20% (w/v) PEG 8000 and 0.1 M sodium cacodylate, pH 6.5, EVAPORATION, temperature 298K
Resolution 2.10 Å R-free 0.249
3MRO Crystal Structure of MHC class I HLA-A2 molecule complexed with Melan-A MART1 decapeptide variant Deposited 2010-04-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain P 26–35（10 aa） Fragment：Melan-A MART1 protein fragment, UNP residues 26-35
Mutation：I5W No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；12% PEG 6000, 0.1M NaCitrate, 0.1M NaCl, 3mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.35 Å R-free 0.279
3MRP Crystal Structure of MHC class I HLA-A2 molecule complexed with Melan-A MART1 decapeptide variant Deposited 2010-04-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain P 26–35（10 aa） Fragment：Melan-A MART1 protein fragment, UNP residues 26-35
Mutation：I5L/L8N No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；13% PEG 6000, 0.1M NaCitrate, 0.1M NaCl, 2.61mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.10 Å R-free 0.227
3MRQ Crystal Structure of MHC class I HLA-A2 molecule complexed with Melan-A MART1 decapeptide variant Deposited 2010-04-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain P 26–35（10 aa） Fragment：Melan-A MART1 protein fragment, UNP residues 26-35
Mutation：I5L/L8N No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；17% PEG 6000, 0.1M NaCitrate, 0.1M NaCl, 2.61mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.235
4EUP The complex between TCR JKF6 and human Class I MHC HLA-A2 presenting the MART-1(27-35)(A27L) peptide Deposited 2012-04-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain F 27–35（9 aa） Fragment：UNP residues 27-35
Mutation：A28L No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M Bis-Tris, 16% PEG10000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.88 Å R-free 0.295
4EUP The complex between TCR JKF6 and human Class I MHC HLA-A2 presenting the MART-1(27-35)(A27L) peptide Deposited 2012-04-25 Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 27–35（9 aa） Fragment：UNP residues 27-35
Mutation：A28L No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M Bis-Tris, 16% PEG10000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.88 Å R-free 0.295
4L3E The complex between high affinity TCR DMF5(alpha-D26Y,beta-L98W) and human Class I MHC HLA-A2 with the bound MART-1(26-35)(A27L) peptide Deposited 2013-06-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 26–35（10 aa） Fragment：UNP residues 26-35
Mutation：A27L No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；12% PEG3350, 0.1 M Tris-HCl, 0.25 M magnesium chloride, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.56 Å R-free 0.266
4QOK Structural basis for ineffective T-cell responses to MHC anchor residue improved heteroclitic peptides Deposited 2014-06-20 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 26–35（10 aa）
Not recorded EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1 M Sodium Cacodylate, pH 6.5, 15% PEG 4000, 15% Glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 3.00 Å R-free 0.262
4WJ5 Structure of HLA-A2 in complex with an altered peptide ligands based on Mart-1 variant epitope Deposited 2014-09-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 26–35（10 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；Good diffracting crystals were obtained by streak seeding
Resolution 1.65 Å R-free 0.179
4WJ5 Structure of HLA-A2 in complex with an altered peptide ligands based on Mart-1 variant epitope Deposited 2014-09-29 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain F 26–35（10 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；Good diffracting crystals were obtained by streak seeding
Resolution 1.65 Å R-free 0.179
6D78 The complex between high-affinity TCR DMF5(alpha-D26Y,beta-L98W) and human Class I MHC HLA-A2 with the bound MART-1(27-35)peptide Deposited 2018-04-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 27–35（9 aa） Fragment：peptide (UNP residues 27-35)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1 M Tris, 12% PEG6000, 0.2 M magnesium chloride
Resolution 2.35 Å R-free 0.255
6DKP The complex among DMF5(alpha-D26Y, alpha-Y50A,beta-L98W) TCR, human Class I MHC HLA-A2 and MART-1(26-35)(A27L) peptide Deposited 2018-05-30 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 26–35（10 aa） Fragment：residues 26-35
Mutation：A27L No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；12% Peg 3350, 250mM MgCl2, 0.1M HEPES
Resolution 2.97 Å R-free 0.286
7TR4 MA2-MART1-HLAA0201 Deposited 2022-01-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain P 26–35（10 aa） Fragment：residues 26-35
Not recorded GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；20% PEG-6000 0.1M Tris (pH8) 0.2M MgCl2
Resolution 2.30 Å R-free 0.267
9O5S minibinder-antigen complex BXMart1-3-MART1-HLA*A02 Deposited 2025-04-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain P 26–35（10 aa） Fragment：residues 26-35
Not recorded GOL GLYCEROL × 15 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.2M potassium thiocyanate, 20% w/v PEG 3350
Resolution 2.27 Å R-free 0.234
9O5S minibinder-antigen complex BXMart1-3-MART1-HLA*A02 Deposited 2025-04-10 Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain E 26–35（10 aa） Fragment：residues 26-35
Not recorded GOL GLYCEROL × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.2M potassium thiocyanate, 20% w/v PEG 3350
Resolution 2.27 Å R-free 0.234
9O5S minibinder-antigen complex BXMart1-3-MART1-HLA*A02 Deposited 2025-04-10 Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain J 26–35（10 aa） Fragment：residues 26-35
Not recorded GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.2M potassium thiocyanate, 20% w/v PEG 3350
Resolution 2.27 Å R-free 0.234
9O5S minibinder-antigen complex BXMart1-3-MART1-HLA*A02 Deposited 2025-04-10 Assembly 4 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain N 26–35（10 aa） Fragment：residues 26-35
Not recorded GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.2M potassium thiocyanate, 20% w/v PEG 3350
Resolution 2.27 Å R-free 0.234

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.