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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：Q08465 New Search
6PDB entries
9Biological assembly
9chain/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
2JMI NMR solution structure of PHD finger fragment of Yeast Yng1 protein in free state Deposited 2006-11-15 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 141–219（79 aa） Fragment：PHD finger
Not recorded ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 7.5；20 K；Ionic strength (raw mmCIF value) 50；Pressure ambient
NMR sample composition 0.54 mM [U-13C, U-15N] YNG1_PHD, 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.6 mM [U-15N] YNG1_PHD, 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.54 mM [U-13C, U-15N] YNG1_PHD, 100% D2O | 100% D2O
Resolution not provided
2JMJ NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide Deposited 2006-11-15 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 141–219（79 aa） Fragment：PHD finger
Not recorded ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 7.5；20 K；Ionic strength (raw mmCIF value) 50；Pressure ambient
NMR sample composition 0.52 mM [U-15N] YNG1_PHD, 2.5 mM H3(1-9)K4me3, 2 mM DTT, 50 mM potassium chloride, 20 mM sodium phosphate, 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.48 mM [U-13C; U-15N] YNG1_PHD, 2.5 mM H3(1-9)K4me3, 2 mM DTT, 50 mM potassium chloride, 20 mM sodium phosphate, 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
8U77 Crystal structure of Taf14 in complex with Yng1 Deposited 2023-09-14 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 113–124（12 aa） Fragment：UNP residues 113-124
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；40% PEG 400, 0.1 M Tris pH 8.5, 0.2 M LiSO4
Resolution 1.93 Å R-free 0.221
8U77 Crystal structure of Taf14 in complex with Yng1 Deposited 2023-09-14 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 113–124（12 aa） Fragment：UNP residues 113-124
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；40% PEG 400, 0.1 M Tris pH 8.5, 0.2 M LiSO4
Resolution 1.93 Å R-free 0.221
8U77 Crystal structure of Taf14 in complex with Yng1 Deposited 2023-09-14 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain F 113–124（12 aa） Fragment：UNP residues 113-124
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；40% PEG 400, 0.1 M Tris pH 8.5, 0.2 M LiSO4
Resolution 1.93 Å R-free 0.221
8U77 Crystal structure of Taf14 in complex with Yng1 Deposited 2023-09-14 Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain H 113–124（12 aa） Fragment：UNP residues 113-124
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；40% PEG 400, 0.1 M Tris pH 8.5, 0.2 M LiSO4
Resolution 1.93 Å R-free 0.221
9UUO The NuA3 histone acetyltransferase complex Deposited 2025-05-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 1–219（219 aa）
Not recorded ZN ZINC ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.68 Å
9UUS The NuA3 histone acetyltransferase complex bound to acetyl-CoA and H3 tail Deposited 2025-05-08 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain C 1–219（219 aa）
Not recorded ZN ZINC ION × 5 ACO ACETYL COENZYME *A × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9VKW Cryo-EM structure of the NuA3 complex bound to Ace-coenzyme A Deposited 2025-06-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 1–219（219 aa）
Not recorded ZN ZINC ION × 4 ACO ACETYL COENZYME *A × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.13 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.