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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：P56524 New Search
18PDB entries
32Biological assembly
39chain/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
2H8N Structure of a glutamine-rich domain from histone deacetylase 4 Deposited 2006-06-07 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 62–153（92 aa） Fragment：N-terminal glutamine-rich Domain, residues 62-129
Chain B 62–153（92 aa） Fragment：N-terminal glutamine-rich Domain, residues 62-129
Chain C 62–153（92 aa） Fragment：N-terminal glutamine-rich Domain, residues 62-129
Chain D 62–153（92 aa） Fragment：N-terminal glutamine-rich Domain, residues 62-129
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；291 K；0.825M LITHIUM SULFATE, 55mM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K, pH 7.50
Resolution 2.60 Å R-free 0.307
2O94 The 97H/F mutant Structure of a glutamine-rich domain from histone deacetylase 4 Deposited 2006-12-13 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 62–153（92 aa） Fragment：N-terminal glutamine-rich domain, residues 62-129
Chain B 62–153（92 aa） Fragment：N-terminal glutamine-rich domain, residues 62-129
Chain C 62–153（92 aa） Fragment：N-terminal glutamine-rich domain, residues 62-129
Chain D 62–153（92 aa） Fragment：N-terminal glutamine-rich domain, residues 62-129
Mutation：H97F Mutation：H97F Mutation：H97F Mutation：H97F No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.540M LITHIUM SULFATE 55mM HEPES PH7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 3.00 Å R-free 0.327
2VQJ Structure of HDAC4 catalytic domain bound to a trifluoromethylketone inhbitor Deposited 2008-03-17 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Not recorded DIO 1,4-DIETHYLENE DIOXIDE × 1 K POTASSIUM ION × 2 SO4 SULFATE ION × 3 TFG 2,2,2-TRIFLUORO-1-{5-[(3-PHENYL-5,6-DIHYDROIMIDAZO[1,2-A]PYRAZIN-7(8H)-YL)CARBONYL]THIOPHEN-2-YL}ETHANE-1,1-DIOL × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；1.6M AMMONIUM SULPHATE, 0.1M MES PH 6.5, 10% DIOXANE 1MM DTT
Resolution 2.10 Å R-free 0.276
2VQM Structure of HDAC4 catalytic domain bound to a hydroxamic acid inhbitor Deposited 2008-03-17 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Not recorded K POTASSIUM ION × 2 HA3 N-hydroxy-5-[(3-phenyl-5,6-dihydroimidazo[1,2-a]pyrazin-7(8H)-yl)carbonyl]thiophene-2-carboxamide × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.4；1.5M AMMONIUM SULPHATE 0.1M MES PH 6.4 10% DIOXANE 1MM DTT
Resolution 1.80 Å R-free 0.256
2VQO Structure of HDAC4 catalytic domain with a gain-of-function muation bound to a trifluoromethylketone inhbitor Deposited 2008-03-18 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Mutation：YES SO4 SULFATE ION × 2 K POTASSIUM ION × 2 TFG 2,2,2-TRIFLUORO-1-{5-[(3-PHENYL-5,6-DIHYDROIMIDAZO[1,2-A]PYRAZIN-7(8H)-YL)CARBONYL]THIOPHEN-2-YL}ETHANE-1,1-DIOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；1.6M AMMONIUM SULPHATE, 0.1M MES PH 6.5, 10% DIOXANE, 1MM DTT
Resolution 2.15 Å R-free 0.250
2VQO Structure of HDAC4 catalytic domain with a gain-of-function muation bound to a trifluoromethylketone inhbitor Deposited 2008-03-18 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Mutation：YES SO4 SULFATE ION × 1 K POTASSIUM ION × 2 TFG 2,2,2-TRIFLUORO-1-{5-[(3-PHENYL-5,6-DIHYDROIMIDAZO[1,2-A]PYRAZIN-7(8H)-YL)CARBONYL]THIOPHEN-2-YL}ETHANE-1,1-DIOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；1.6M AMMONIUM SULPHATE, 0.1M MES PH 6.5, 10% DIOXANE, 1MM DTT
Resolution 2.15 Å R-free 0.250
2VQQ Structure of HDAC4 catalytic domain (a double cysteine-to-alanine mutant) bound to a trifluoromethylketone inhbitor Deposited 2008-03-18 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Mutation：YES SO4 SULFATE ION × 2 K POTASSIUM ION × 2 TFG 2,2,2-TRIFLUORO-1-{5-[(3-PHENYL-5,6-DIHYDROIMIDAZO[1,2-A]PYRAZIN-7(8H)-YL)CARBONYL]THIOPHEN-2-YL}ETHANE-1,1-DIOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；1.6M AMMONIUM SULPHATE, 0.1M MES PH 6.5, 10% DIOXANE 1MM DTT
Resolution 1.90 Å R-free 0.221
2VQQ Structure of HDAC4 catalytic domain (a double cysteine-to-alanine mutant) bound to a trifluoromethylketone inhbitor Deposited 2008-03-18 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Mutation：YES SO4 SULFATE ION × 1 K POTASSIUM ION × 2 TFG 2,2,2-TRIFLUORO-1-{5-[(3-PHENYL-5,6-DIHYDROIMIDAZO[1,2-A]PYRAZIN-7(8H)-YL)CARBONYL]THIOPHEN-2-YL}ETHANE-1,1-DIOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；1.6M AMMONIUM SULPHATE, 0.1M MES PH 6.5, 10% DIOXANE 1MM DTT
Resolution 1.90 Å R-free 0.221
2VQV Structure of HDAC4 catalytic domain with a gain-of-function mutation bound to a hydroxamic acid inhibitor Deposited 2008-03-19 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Mutation：YES SO4 SULFATE ION × 1 K POTASSIUM ION × 2 HA3 N-hydroxy-5-[(3-phenyl-5,6-dihydroimidazo[1,2-a]pyrazin-7(8H)-yl)carbonyl]thiophene-2-carboxamide × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.1M MES PH 6.5, 1.6M AMMONIUM SULPHATE, 10% DIOXANE 1MM DTT
Resolution 3.30 Å R-free 0.265
2VQV Structure of HDAC4 catalytic domain with a gain-of-function mutation bound to a hydroxamic acid inhibitor Deposited 2008-03-19 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Mutation：YES SO4 SULFATE ION × 3 K POTASSIUM ION × 2 HA3 N-hydroxy-5-[(3-phenyl-5,6-dihydroimidazo[1,2-a]pyrazin-7(8H)-yl)carbonyl]thiophene-2-carboxamide × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.1M MES PH 6.5, 1.6M AMMONIUM SULPHATE, 10% DIOXANE 1MM DTT
Resolution 3.30 Å R-free 0.265
2VQW Structure of inhibitor-free HDAC4 catalytic domain (with gain-of- function mutation His332Tyr) Deposited 2008-03-19 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain G 648–1057（410 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1057
Mutation：YES K POTASSIUM ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；0.1M HEPES PH 7.5, 18% PEG 10000, 1MM DTT
Resolution 3.00 Å R-free 0.261
3UXG Crystal structure of RFXANK Deposited 2011-12-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 343–359（17 aa）
Not recorded UNX UNKNOWN LIGAND × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；25% PEG3350, 0.2M sodium chloride, 0.1M HEPES, pH 7.5, vapor diffusion, sitting drop, temperature 291K
Resolution 1.85 Å R-free 0.222
3UXG Crystal structure of RFXANK Deposited 2011-12-05 Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 343–359（17 aa）
Not recorded UNX UNKNOWN LIGAND × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；25% PEG3350, 0.2M sodium chloride, 0.1M HEPES, pH 7.5, vapor diffusion, sitting drop, temperature 291K
Resolution 1.85 Å R-free 0.222
3UZD Crystal structure of 14-3-3 GAMMA Deposited 2011-12-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain B 343–359（17 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) NO3 NITRATE ION × 12 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.3M Mg (OAc)2, 20% PEG3350, vapor diffusion, hanging drop, temperature 291K
Resolution 1.86 Å R-free 0.230
3UZD Crystal structure of 14-3-3 GAMMA Deposited 2011-12-07 Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 343–359（17 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) NO3 NITRATE ION × 6 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.3M Mg (OAc)2, 20% PEG3350, vapor diffusion, hanging drop, temperature 291K
Resolution 1.86 Å R-free 0.230
3UZD Crystal structure of 14-3-3 GAMMA Deposited 2011-12-07 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 343–359（17 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) NO3 NITRATE ION × 3 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.3M Mg (OAc)2, 20% PEG3350, vapor diffusion, hanging drop, temperature 291K
Resolution 1.86 Å R-free 0.230
3V31 Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2 Deposited 2011-12-12 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 343–359（17 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；0.1M Bis-Tris, pH 6.5, 0.2M NaCl, 25% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.57 Å R-free 0.204
4CBT Design, synthesis, and biological evaluation of potent and selective Class IIa HDAC inhibitors as a potential therapy for Huntington's disease Deposited 2013-10-16 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1033（386 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1033
Not recorded 9F4 (1R,2R,3R)-2-[4-(5-fluoranylpyrimidin-2-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.1 M BISTRIS PH 6.5, 22% PEG MME 5000
Resolution 3.03 Å R-free 0.273
4CBT Design, synthesis, and biological evaluation of potent and selective Class IIa HDAC inhibitors as a potential therapy for Huntington's disease Deposited 2013-10-16 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 648–1033（386 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1033
Not recorded 9F4 (1R,2R,3R)-2-[4-(5-fluoranylpyrimidin-2-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.1 M BISTRIS PH 6.5, 22% PEG MME 5000
Resolution 3.03 Å R-free 0.273
4CBT Design, synthesis, and biological evaluation of potent and selective Class IIa HDAC inhibitors as a potential therapy for Huntington's disease Deposited 2013-10-16 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 648–1033（386 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1033
Not recorded 9F4 (1R,2R,3R)-2-[4-(5-fluoranylpyrimidin-2-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.1 M BISTRIS PH 6.5, 22% PEG MME 5000
Resolution 3.03 Å R-free 0.273
4CBY Design, synthesis, and biological evaluation of potent and selective Class IIa HDAC inhibitors as a potential therapy for Huntington's disease Deposited 2013-10-17 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1033（386 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1033
Mutation：YES KEE (1R,2R,3R)-2-[4-(1,3-oxazol-5-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；18-24% (W/V) PEG 3350, 0.2 M NACL AND 100 MM BIS-TRIS PH 5.5
Resolution 2.72 Å R-free 0.246
4CBY Design, synthesis, and biological evaluation of potent and selective Class IIa HDAC inhibitors as a potential therapy for Huntington's disease Deposited 2013-10-17 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 648–1033（386 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1033
Mutation：YES KEE (1R,2R,3R)-2-[4-(1,3-oxazol-5-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；18-24% (W/V) PEG 3350, 0.2 M NACL AND 100 MM BIS-TRIS PH 5.5
Resolution 2.72 Å R-free 0.246
4CBY Design, synthesis, and biological evaluation of potent and selective Class IIa HDAC inhibitors as a potential therapy for Huntington's disease Deposited 2013-10-17 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 648–1033（386 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1033
Mutation：YES KEE (1R,2R,3R)-2-[4-(1,3-oxazol-5-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；18-24% (W/V) PEG 3350, 0.2 M NACL AND 100 MM BIS-TRIS PH 5.5
Resolution 2.72 Å R-free 0.246
4CBY Design, synthesis, and biological evaluation of potent and selective Class IIa HDAC inhibitors as a potential therapy for Huntington's disease Deposited 2013-10-17 Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain D 648–1033（386 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 648-1033
Mutation：YES KEE (1R,2R,3R)-2-[4-(1,3-oxazol-5-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；18-24% (W/V) PEG 3350, 0.2 M NACL AND 100 MM BIS-TRIS PH 5.5
Resolution 2.72 Å R-free 0.246
5A2S Potent, selective and CNS-penetrant tetrasubstituted cyclopropane class IIa histone deacetylase (HDAC) inhibitors Deposited 2015-05-22 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1033（386 aa） Fragment：HISTONE DEACETYLASE DOMAIN, RESIDUES 648-1033
Mutation：YES OTF (1S,2S,3S)-1-fluoranyl-2-[4-(5-fluoranylpyrimidin-2-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 24% W/V PEG 3350, 0.2 M AMMONIUM ACETATE, 0.1 M BIS-TRIS PH 5.5, 10 MM PROLINE
Resolution 2.65 Å R-free 0.256
5A2S Potent, selective and CNS-penetrant tetrasubstituted cyclopropane class IIa histone deacetylase (HDAC) inhibitors Deposited 2015-05-22 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 648–1033（386 aa） Fragment：HISTONE DEACETYLASE DOMAIN, RESIDUES 648-1033
Mutation：YES OTF (1S,2S,3S)-1-fluoranyl-2-[4-(5-fluoranylpyrimidin-2-yl)phenyl]-N-oxidanyl-3-phenyl-cyclopropane-1-carboxamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 24% W/V PEG 3350, 0.2 M AMMONIUM ACETATE, 0.1 M BIS-TRIS PH 5.5, 10 MM PROLINE
Resolution 2.65 Å R-free 0.256
5ZOO Crystal structure of histone deacetylase 4 (HDAC4) in complex with a SMRT corepressor SP1 fragment Deposited 2018-04-13 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 652–1053（402 aa） Fragment：UNP residues 652-1052
Mutation：H976Y K POTASSIUM ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7.5；295 K；PEG 3350, iso-propanol
Resolution 1.85 Å R-free 0.175
5ZOP Crystal structure of histone deacetylase 4 (HDAC4) in complex with a SMRT corepressor SP2 fragment Deposited 2018-04-13 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 652–1050（399 aa） Fragment：UNP residues 652-1050
Mutation：H976Y K POTASSIUM ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7.5；295 K；PEG 3350, iso-propanol
Resolution 2.70 Å R-free 0.235
6FYZ Development and characterization of a CNS-penetrant benzhydryl hydroxamic acid class IIa histone deacetylase inhibitor Deposited 2018-03-13 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 648–1033（386 aa）
Not recorded EBE (2~{S})-2-(2-fluorophenyl)-2-[4-(2-methylpyrimidin-5-yl)phenyl]-~{N}-oxidanyl-ethanamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M BisTris, 18 to 24% PEG MME 5000
Resolution 2.15 Å R-free 0.228
6FYZ Development and characterization of a CNS-penetrant benzhydryl hydroxamic acid class IIa histone deacetylase inhibitor Deposited 2018-03-13 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 648–1033（386 aa）
Not recorded EBE (2~{S})-2-(2-fluorophenyl)-2-[4-(2-methylpyrimidin-5-yl)phenyl]-~{N}-oxidanyl-ethanamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M BisTris, 18 to 24% PEG MME 5000
Resolution 2.15 Å R-free 0.228
6FYZ Development and characterization of a CNS-penetrant benzhydryl hydroxamic acid class IIa histone deacetylase inhibitor Deposited 2018-03-13 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 648–1033（386 aa）
Not recorded EBE (2~{S})-2-(2-fluorophenyl)-2-[4-(2-methylpyrimidin-5-yl)phenyl]-~{N}-oxidanyl-ethanamide × 1 ZN ZINC ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M BisTris, 18 to 24% PEG MME 5000
Resolution 2.15 Å R-free 0.228
7XUZ Crystal structure of a HDAC4-MEF2A-DNA ternary complex Deposited 2022-05-20 Assembly 1 Protein–DNA Heteromer；Protein × 6 PDB declaration: decameric（10） Consistent with all polymers
Chain A 62–192（131 aa）
Chain B 62–192（131 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0 mM HEPES pH 7.5, 0.2 M NaCl, 3% (v/v) PEG 4000
Resolution 3.59 Å R-free 0.298

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.