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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：Q9NT62 New Search
3PDB entries
7Biological assembly
11chain/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
4NAW Crystal Structure of Human ATG12~ATG5-ATG16N in complex with a fragment of ATG3 Deposited 2013-10-22 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain D 140–170（31 aa） Fragment：UNP residues 140-170
Not recorded SO4 SULFATE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PROTEIN - 10 MG/ML in 0.01M HEPES pH 7.0, 0.15 M NaCl, 0.001 M DTT, RESERVOIR - 0.1M MES pH6.0-6.75, 0.2 M ammonium sulfate, 10-16% PEG 5000 MME, vapor diffusion, sitting drop, temperature 293K
Resolution 2.19 Å R-free 0.215
4NAW Crystal Structure of Human ATG12~ATG5-ATG16N in complex with a fragment of ATG3 Deposited 2013-10-22 Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain H 140–170（31 aa） Fragment：UNP residues 140-170
Not recorded SO4 SULFATE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PROTEIN - 10 MG/ML in 0.01M HEPES pH 7.0, 0.15 M NaCl, 0.001 M DTT, RESERVOIR - 0.1M MES pH6.0-6.75, 0.2 M ammonium sulfate, 10-16% PEG 5000 MME, vapor diffusion, sitting drop, temperature 293K
Resolution 2.19 Å R-free 0.215
4NAW Crystal Structure of Human ATG12~ATG5-ATG16N in complex with a fragment of ATG3 Deposited 2013-10-22 Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain L 140–170（31 aa） Fragment：UNP residues 140-170
Not recorded SO4 SULFATE ION × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PROTEIN - 10 MG/ML in 0.01M HEPES pH 7.0, 0.15 M NaCl, 0.001 M DTT, RESERVOIR - 0.1M MES pH6.0-6.75, 0.2 M ammonium sulfate, 10-16% PEG 5000 MME, vapor diffusion, sitting drop, temperature 293K
Resolution 2.19 Å R-free 0.215
4NAW Crystal Structure of Human ATG12~ATG5-ATG16N in complex with a fragment of ATG3 Deposited 2013-10-22 Assembly 4 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain P 140–170（31 aa） Fragment：UNP residues 140-170
Not recorded SO4 SULFATE ION × 3 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PROTEIN - 10 MG/ML in 0.01M HEPES pH 7.0, 0.15 M NaCl, 0.001 M DTT, RESERVOIR - 0.1M MES pH6.0-6.75, 0.2 M ammonium sulfate, 10-16% PEG 5000 MME, vapor diffusion, sitting drop, temperature 293K
Resolution 2.19 Å R-free 0.215
8FKM Human Atg3 with deletions of residues 1 to 25 and 90 to 190 Deposited 2022-12-21 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–314（314 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) NaCl 150；Pressure 1
NMR sample composition 150 mM NaCl, 50 mM HEPES, 2 mM TCEP, 0.5 mM [U-13C; U-15N] human Atg3, 96% H2O/4% D2O | 96% H2O/4% D2O
NMR sample composition 150 mM NaCl, 50 mM HEPES, 2 mM TCEP, 0.5 mM [U-13C; U-15N] human Atg3, 6.5 mg/mL Pf1 phage, 96% H2O/4% D2O | 96% H2O/4% D2O
NMR sample composition 150 mM NaCl, 50 mM HEPES, 2 mM TCEP, 0.5 mM [U-13C; U-15N] human Atg3, 7 % positive gel, 96% H2O/4% D2O | 96% H2O/4% D2O
NMR sample composition 150 mM NaCl, 50 mM HEPES, 2 mM TCEP, 0.5 mM [U-13C; U-15N] human Atg3, 5 % negative gel, 96% H2O/4% D2O | 96% H2O/4% D2O
NMR sample composition 150 mM NaCl, 50 mM HEPES, 2 mM TCEP, 0.5 mM [U-13C; U-15N] human Atg3, 5 % neutral gel, 96% H2O/4% D2O | 96% H2O/4% D2O
NMR sample composition 150 mM NaCl, 50 mM HEPES, 2 mM TCEP, 0.5 mM [U-13C; U-15N] human Atg3, 100% D2O | 100% D2O
NMR sample composition 150 mM NaCl, 50 mM HEPES, 2 mM TCEP, 0.5 mM [U-13C; U-15N] human Atg3, 92% H2O/8% D2O | 92% H2O/8% D2O
Resolution not provided
9E8P Crystal Structure of GABARAP-ATG3 conjugate Deposited 2024-11-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 26–91（66 aa）
Chain A 148–181（34 aa）
Chain A 193–314（122 aa）
Mutation：C264K Mutation：C264K Mutation：C264K SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277.15 K；0.1 mM Tris pH8.5, 25%(w/v) PEG3550
Resolution 2.70 Å R-free 0.249
9E8P Crystal Structure of GABARAP-ATG3 conjugate Deposited 2024-11-05 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 26–91（66 aa）
Chain B 148–181（34 aa）
Chain B 193–314（122 aa）
Mutation：C264K Mutation：C264K Mutation：C264K EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277.15 K；0.1 mM Tris pH8.5, 25%(w/v) PEG3550
Resolution 2.70 Å R-free 0.249

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.