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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：Q15628 New Search
7PDB entries
7Biological assembly
38chain/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
1F2H SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TNFR1 ASSOCIATED PROTEIN, TRADD. Deposited 2000-05-24 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–169（169 aa） Fragment：N-TERMINAL DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.6；298 K；Ionic strength (raw mmCIF value) 200mM NaCl；Pressure 1
NMR measurement conditions pH 6.6；298 K；Ionic strength (raw mmCIF value) 200mM NaCl；Pressure 1
NMR measurement conditions pH 6.6；298 K；Ionic strength (raw mmCIF value) 200mM NaCl；Pressure 1
NMR sample composition 1.0 mM 15N N-TRADD | 20mM Imidazole pH 6.6 200 mMNaCL 20 mM DTT 0.05%NaN3 90%H2O 10% D2O
NMR sample composition 1.1 mM 15N/13C N-TRADD | 20mM Imidazole pH 6.6 200 mMNaCL 20 mM DTT 0.05%NaN3 90%H2O 10% D2O
NMR sample composition 0.8 mM 15N/13C N-TRADD | 20mM Imidazole pH 6.6 200 mMNaCL 220 mM DTT 0.05%NaN3 100% D2O
Resolution not provided
1F3V Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2 Deposited 2000-06-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–179（179 aa） Fragment：N-TERMINAL DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；VAPOR DIFFUSION, temperature 293K
Resolution 2.00 Å R-free 0.261
5XME Solution structure of C-terminal domain of TRADD Deposited 2017-05-15 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 199–312（114 aa） Fragment：UNP RESIDUES 199-312
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；301 K；Pressure 1
NMR sample composition 0.6 mM U-99% 13C; U-99% 15N;U-98% 2H TRADD DD, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
6AC0 Crystal structure of TRADD death domain GlcNAcylated by EPEC effector NleB Deposited 2018-07-24 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 195–312（118 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；1.6 M Na/KPO4, pH 6.0
Resolution 1.45 Å R-free 0.224
7CSQ Solution structure of the complex between p75NTR-DD and TRADD-DD Deposited 2020-08-16 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 199–312（114 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；301 K；Pressure 1
NMR sample composition 0.2 mM [U-99% 13C; U-99% 15N] p75 neurotrophin receptor death domain, 2 mM [U-99% 13C; U-99% 15N] tumor necrosis factor receptor1-associated death domain protein, 50% H2O/50% D2O | 50% H2O/50% D2O
Resolution not provided
9VGD Helical assembly of TRADD death domain Deposited 2025-06-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 28 PDB declaration: 28-meric（28） Consistent with protein count
Chain A 199–312（114 aa）
Chain B 199–312（114 aa）
Chain C 199–312（114 aa）
Chain E 199–312（114 aa）
Chain F 199–312（114 aa）
Chain H 199–312（114 aa）
Chain I 199–312（114 aa）
Chain J 199–312（114 aa）
Chain K 199–312（114 aa）
Chain M 199–312（114 aa）
Chain N 199–312（114 aa）
Chain Q 199–312（114 aa）
Chain R 199–312（114 aa）
Chain S 199–312（114 aa）
Chain T 199–312（114 aa）
Chain V 199–312（114 aa）
Chain W 199–312（114 aa）
Chain Y 199–312（114 aa）
Chain Z 199–312（114 aa）
Chain b 199–312（114 aa）
Chain c 199–312（114 aa）
Chain e 199–312（114 aa）
Chain f 199–312（114 aa）
Chain g 199–312（114 aa）
Chain h 199–312（114 aa）
Chain j 199–312（114 aa）
Chain k 199–312（114 aa）
Chain l 199–312（114 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9VIN Ternary complex of TNFR1-DD, TRADD-DD and RIPK1-DD Deposited 2025-06-18 Assembly 1 Protein heterocomplex Heteromer；Protein × 31 PDB declaration: 31-meric（31） Consistent with protein count
Chain E 199–312（114 aa）
Chain F 199–312（114 aa）
Chain N 199–312（114 aa）
Chain V 199–312（114 aa）
Chain W 199–312（114 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；100 mM NaCl, 20 mM Tris-HCl pH7.5, 1mM EDTA, 1mM DTT.
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.41 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.