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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：O43914 New Search
5PDB entries
11Biological assembly
17chain/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
2L34 Structure of the DAP12 transmembrane homodimer Deposited 2010-09-06 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 35–67（33 aa） Fragment：UNP RESIDUES 35-67
Chain B 35–67（33 aa） Fragment：UNP RESIDUES 35-67
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 20；Pressure ambient
NMR sample composition 0.5 (dimer) mM [U-100% 13C; U-100% 15N; U-80% 2H] DAP12 transmembrane peptide-1, 20 mM sodium phosphate-2, 25 mM SDS-3, 250 mM Foscholine-14-4, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5 (dimer) mM [U-100% 13C; U-100% 15N] DAP12 transmembrane peptide-5, 20 mM sodium phosphate-6, 25 mM [U-100% 2H] SDS-7, 250 mM [U-100% 2H] Foscholine-14-8, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5 (monomer) mM [U-100% 15N; U-100% 2H] DAP12 transmembrane peptide-9, 0.5 (monomer) mM [U-100% 13C] DAP12 transmembrane peptide-10, 25 mM [U-100% 2H] SDS-11, 250 mM [U-100% 2H] Foscholine-14-12, 20 mM sodium phosphate-13, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5 (dimer) mM [U-10% 13C] DAP12 transmembrane peptide-14, 25 mM [U-100% 2H] SDS-15, 250 mM [U-100% 2H] Foscholine-14-16, 20 mM sodium phosphate-17, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2L35 Structure of the DAP12-NKG2C transmembrane heterotrimer Deposited 2010-09-06 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 35–67（33 aa）
Chain B 35–66（32 aa） Fragment：UNP RESIDUES 35-66
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 20；Pressure ambient
NMR sample composition 0.5-1 mM [U-100% 13C; U-100% 15N; U-80% 2H] DAP12-NKG2C TM-1, 0.5-1 mM DAP12 TM-2, 25 mM SDS-3, 250 mM Foscholine-14-4, 20 mM sodium phosphate-5, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5-1 mM DAP12-NKG2C TM-6, 0.5-1 mM [U-100% 13C; U-100% 15N; U-80% 2H] DAP12 TM-7, 25 mM SDS-8, 250 mM Foscholine-14-9, 20 mM sodium phosphate-10, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5-1 mM [U-100% 13C; U-100% 15N] DAP12-NKG2C TM-11, 0.5-1 mM DAP12 TM-12, 25 mM [U-100% 2H] SDS-13, 250 mM [U-100% 2H] Foscholine-14-14, 20 mM sodium phosphate-15, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5-1 mM DAP12-NKG2C TM-16, 0.5-1 mM [U-100% 13C; U-100% 15N] DAP12 TM-17, 25 mM [U-100% 2H] SDS-18, 250 mM [U-100% 2H] Foscholine-14-19, 20 mM sodium phosphate-20, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5-1 mM [U-100% 15N; U-100% 2H] DAP12-NKG2C TM-21, 0.5-1 mM [U-10% 13C] DAP12 TM-22, 25 mM [U-100% 2H] SDS-23, 250 mM [U-100% 2H] Foscholine-14-24, 20 mM sodium phosphate-25, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5-1 mM [U-10% 13C] DAP12-NKG2C TM-26, 0.5-1 mM [U-100% 15N; U-90% 2H] DAP12 TM-27, 25 mM [U-100% 2H] SDS-28, 250 mM [U-100% 2H] Foscholine-14-29, 20 mM sodium phosphate-30, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
4WO1 Crystal structure of the DAP12 transmembrane domain in lipid cubic phase Deposited 2014-10-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 35–67（33 aa） Fragment：UNP residues 35-67
Chain D 35–67（33 aa） Fragment：UNP residues 35-67
Mutation：M21V Mutation：M21V CA CALCIUM ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 3 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 6.07；293 K；0.1 M bis-tris propane chloride pH 6.07, 19.7 %w/v PEG 3350, 0.27 M calcium chloride
Resolution 2.14 Å R-free 0.296
4WO1 Crystal structure of the DAP12 transmembrane domain in lipid cubic phase Deposited 2014-10-15 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 35–67（33 aa） Fragment：UNP residues 35-67
Chain C 35–67（33 aa） Fragment：UNP residues 35-67
Mutation：M21V Mutation：M21V OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 3 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 6.07；293 K；0.1 M bis-tris propane chloride pH 6.07, 19.7 %w/v PEG 3350, 0.27 M calcium chloride
Resolution 2.14 Å R-free 0.296
4WOL Crystal Structure of the DAP12 transmembrane domain in lipidic cubic phase Deposited 2014-10-16 Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 35–67（33 aa） Fragment：UNP residues 35-67
Chain B 35–67（33 aa） Fragment：UNP residues 35-67
Chain C 35–67（33 aa） Fragment：UNP residues 35-67
Mutation：M21V Mutation：M21V Mutation：M21V K POTASSIUM ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；12.4% w/v PEG 3350, 0.149 M potassium thiocyanate
Resolution 1.77 Å R-free 0.223
7Q5W The tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM peptide Deposited 2021-11-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain JJJ 88–107（20 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME
Resolution 2.20 Å R-free 0.266
7Q5W The tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM peptide Deposited 2021-11-04 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain LLL 88–107（20 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME
Resolution 2.20 Å R-free 0.266
7Q5W The tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM peptide Deposited 2021-11-04 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain KKK 88–107（20 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME
Resolution 2.20 Å R-free 0.266
7Q5W The tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM peptide Deposited 2021-11-04 Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain GGG 88–107（20 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME
Resolution 2.20 Å R-free 0.266
7Q5W The tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM peptide Deposited 2021-11-04 Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain III 88–107（20 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 1 P4G 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME
Resolution 2.20 Å R-free 0.266
7Q5W The tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM peptide Deposited 2021-11-04 Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain HHH 88–107（20 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME
Resolution 2.20 Å R-free 0.266

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.