SAXSdb — 7yfp

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin

Saccharomyces cerevisiae

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 4–375	Not recorded	ARP4 isoform 1 × 1 （A0A6A5PX31） Chromatin modification-related protein EAF1 × 1 （A0A8H8UNQ6） SWR1-complex protein 4 × 1 （A0A8H4F9Y4） Enhancer of polycomb-like protein 1 × 1 （P43572） Transcription-associated protein 1 × 1 （P38811） ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 7YFP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1YAG STRUCTURE OF THE YEAST ACTIN-HUMAN GELSOLIN SEGMENT 1 COMPLEX Deposited 1998-10-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–375（375 aa）	Not recorded	MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.50	Resolution 1.90 Å R-free 0.231
1YAG STRUCTURE OF THE YEAST ACTIN-HUMAN GELSOLIN SEGMENT 1 COMPLEX Deposited 1998-10-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–375（375 aa）	Not recorded	MG MAGNESIUM ION × 2 SO4 SULFATE ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.50	Resolution 1.90 Å R-free 0.231
1YVN THE YEAST ACTIN VAL 159 ASN MUTANT COMPLEX WITH HUMAN GELSOLIN SEGMENT 1. Deposited 1999-03-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–375（375 aa）	Mutation：V159N	MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.1 M HEPES, 1.60 M (NH4)2SO4, 2 MM MG-ATP, PH=8.0.	Resolution 2.10 Å R-free 0.235
1YVN THE YEAST ACTIN VAL 159 ASN MUTANT COMPLEX WITH HUMAN GELSOLIN SEGMENT 1. Deposited 1999-03-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–375（375 aa）	Mutation：V159N	MG MAGNESIUM ION × 2 SO4 SULFATE ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.1 M HEPES, 1.60 M (NH4)2SO4, 2 MM MG-ATP, PH=8.0.	Resolution 2.10 Å R-free 0.235
5NBL Crystal structure of the Arp4-N-actin(APO-state) heterodimer bound by a nanobody Deposited 2017-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–375（375 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 mM ADP, 0.2 mM CaCl2, 1.3-1.5 M sodium malonate at pH 6.0, Subtilisin (1/6000; w(subtilisin)/w(protein))	Resolution 2.80 Å R-free 0.204
5NBL Crystal structure of the Arp4-N-actin(APO-state) heterodimer bound by a nanobody Deposited 2017-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–375（375 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 mM ADP, 0.2 mM CaCl2, 1.3-1.5 M sodium malonate at pH 6.0, Subtilisin (1/6000; w(subtilisin)/w(protein))	Resolution 2.80 Å R-free 0.204
5NBM Crystal structure of the Arp4-N-actin(ATP-state) heterodimer bound by a nanobody Deposited 2017-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–375（375 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 mM ATP, 0.2 mM CaCl2, 1.3-1.5 M sodium malonate pH 6.0, Subtilisin (1/6000; w(subtilisin)/w(protein))	Resolution 3.40 Å R-free 0.193
5NBM Crystal structure of the Arp4-N-actin(ATP-state) heterodimer bound by a nanobody Deposited 2017-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–375（375 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 mM ATP, 0.2 mM CaCl2, 1.3-1.5 M sodium malonate pH 6.0, Subtilisin (1/6000; w(subtilisin)/w(protein))	Resolution 3.40 Å R-free 0.193
5NBN Crystal structure of the Arp4-N-actin-Arp8-Ino80HSA module of INO80 Deposited 2017-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–375（375 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 LAR LATRUNCULIN A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M sodium citrate tribasic dihydrate, 18% (w/v) polyethylene glycol 3,350, latrunculin A solved in DMSO molar ration 1:1.5 (protein : latrunculin A)	Resolution 4.00 Å R-free 0.242
5NBN Crystal structure of the Arp4-N-actin-Arp8-Ino80HSA module of INO80 Deposited 2017-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–375（375 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 LAR LATRUNCULIN A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M sodium citrate tribasic dihydrate, 18% (w/v) polyethylene glycol 3,350, latrunculin A solved in DMSO molar ration 1:1.5 (protein : latrunculin A)	Resolution 4.00 Å R-free 0.242
5Y81 NuA4 TEEAA sub-complex Deposited 2017-08-18	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain G 1–375（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.70 Å
7VVY TRA module of NuA4 Deposited 2021-11-09	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain G 1–375（375 aa）	Not recorded	MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.10 Å
7VVZ NuA4 bound to the nucleosome Deposited 2021-11-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain G 1–375（375 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME A × 1 MG MAGNESIUM ION × 2 ATP* ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 8.80 Å
7YFN Core module of the NuA4 complex in S. cerevisiae Deposited 2022-07-08	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 4–375（372 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8A5A Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of INO80 Deposited 2022-06-14	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain V 1–375（375 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8A5O Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of S. cerevisiae INO80 Deposited 2022-06-15	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain V 1–375（375 aa）	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8ESC Structure of the Yeast NuA4 Histone Acetyltransferase Complex Deposited 2022-10-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–375（375 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9GO5 CryoEM Reconstruction of Yeast ADP-Actin Filament at 2.5 A resolution. Deposited 2024-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–375（375 aa） Chain B 1–375（375 aa） Chain C 1–375（375 aa） Chain D 1–375（375 aa） Chain E 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8；50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 10 mM Tris cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å

13 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACT_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–372； UniProt 4–375

ARP4 isoform 1

Saccharomyces cerevisiae

UniProt A0A6A5PX31

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain B； UniProt 8–488	Not recorded	Actin × 1 （P60010） Chromatin modification-related protein EAF1 × 1 （A0A8H8UNQ6） SWR1-complex protein 4 × 1 （A0A8H4F9Y4） Enhancer of polycomb-like protein 1 × 1 （P43572） Transcription-associated protein 1 × 1 （P38811） ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 7YFP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7YFN Core module of the NuA4 complex in S. cerevisiae Deposited 2022-07-08	Different construct Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–489（489 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A6A5PX31_YEASX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–481； UniProt 8–488

Chromatin modification-related protein EAF1

Saccharomyces cerevisiae

UniProt A0A8H8UNQ6

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain D； UniProt 1–982	Not recorded	Actin × 1 （P60010） ARP4 isoform 1 × 1 （A0A6A5PX31） SWR1-complex protein 4 × 1 （A0A8H4F9Y4） Enhancer of polycomb-like protein 1 × 1 （P43572） Transcription-associated protein 1 × 1 （P38811） ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 7YFP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7YFN Core module of the NuA4 complex in S. cerevisiae Deposited 2022-07-08	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–982（982 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A8H8UNQ6_YEASX
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain D； PDBConstruct 1–982； UniProt 1–982

SWR1-complex protein 4

Saccharomyces cerevisiae

UniProt A0A8H4F9Y4

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain E； UniProt 1–476	Not recorded	Actin × 1 （P60010） ARP4 isoform 1 × 1 （A0A6A5PX31） Chromatin modification-related protein EAF1 × 1 （A0A8H8UNQ6） Enhancer of polycomb-like protein 1 × 1 （P43572） Transcription-associated protein 1 × 1 （P38811） ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 7YFP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7YFN Core module of the NuA4 complex in S. cerevisiae Deposited 2022-07-08	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 1–476（476 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A8H4F9Y4_YEASX
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain E； PDBConstruct 1–476； UniProt 1–476

Enhancer of polycomb-like protein 1

Saccharomyces cerevisiae

UniProt P43572

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain F； UniProt 1–832	Not recorded	Actin × 1 （P60010） ARP4 isoform 1 × 1 （A0A6A5PX31） Chromatin modification-related protein EAF1 × 1 （A0A8H8UNQ6） SWR1-complex protein 4 × 1 （A0A8H4F9Y4） Transcription-associated protein 1 × 1 （P38811） ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 7YFP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain G 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain N 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9T Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 121–400（280 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
5J9T Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 121–400（280 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
5J9T Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain K 121–400（280 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain N 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 121–400（280 aa） Fragment：UNP residues 121-400	Not recorded	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 121–400（280 aa） Fragment：UNP residues 121-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain K 121–400（280 aa） Fragment：UNP residues 121-400	Not recorded	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
7VVU NuA4 HAT module bound to the nucleosome Deposited 2021-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 13 PDB declaration: pentadecameric	Chain T 1–832（832 aa） Chain X 1–832（832 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME *A × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.40 Å
7VVY TRA module of NuA4 Deposited 2021-11-09	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain H 1–832（832 aa）	Not recorded	MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.10 Å
7VVZ NuA4 bound to the nucleosome Deposited 2021-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain H 1–832（832 aa） Chain T 1–832（832 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME A × 1 MG MAGNESIUM ION × 2 ATP* ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 8.80 Å
7YFN Core module of the NuA4 complex in S. cerevisiae Deposited 2022-07-08	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain F 1–832（832 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8ESC Structure of the Yeast NuA4 Histone Acetyltransferase Complex Deposited 2022-10-13	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 1–832（832 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

9 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EPL1_YEAST
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain F； PDBConstruct 1–832； UniProt 1–832

Transcription-associated protein 1

Saccharomyces cerevisiae

UniProt P38811

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain T； UniProt 1–3744	Not recorded	Actin × 1 （P60010） ARP4 isoform 1 × 1 （A0A6A5PX31） Chromatin modification-related protein EAF1 × 1 （A0A8H8UNQ6） SWR1-complex protein 4 × 1 （A0A8H4F9Y4） Enhancer of polycomb-like protein 1 × 1 （P43572） ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 7YFP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5OJS Cryo-EM structure of the SAGA and NuA4 coactivator subunit Tra1 Deposited 2017-07-24	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain T 1–3744（3744 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Two subsequent applications of protein were required to achieve the desired particle density on grids. Each application was followed by 20 sec waiting time, with a short 0.5 sec blotting after first application and 5 sec blotting after the second.	Resolution 3.70 Å
5Y81 NuA4 TEEAA sub-complex Deposited 2017-08-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–2627（2627 aa） Fragment：UNP residues 1-2627 Chain B 2630–3744（1115 aa） Fragment：UNP residues 2630-3744	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.70 Å
6IG9 Tra1 subunit from Saccharomyces cerevisiae SAGA complex Deposited 2018-09-25	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain T 1–3744（3744 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8.5；20mM HEPES pH 8.5 150mM Nacl cryo-EM vitrification conditions Cryogen ETHANE；Blot for 4 seconds and wait for 30 seconds before plunging	Resolution 4.60 Å
6T9I cryo-EM structure of transcription coactivator SAGA Deposited 2019-10-28	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain T 1–3744（3744 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；Solution were made from stock solution cryo-EM vitrification conditions Cryogen ETHANE；blot for 4 seconds before plunging	Resolution 3.90 Å
6T9J SAGA Tra1 module Deposited 2019-10-28	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain T 1–3744（3744 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；Solution were made from stock solution cryo-EM vitrification conditions Cryogen ETHANE；blot for 4 seconds before plunging	Resolution 3.40 Å
7VVY TRA module of NuA4 Deposited 2021-11-09	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain L 1–3744（3744 aa）	Not recorded	MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.10 Å
7VVZ NuA4 bound to the nucleosome Deposited 2021-11-09	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain L 1–3744（3744 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME A × 1 MG MAGNESIUM ION × 2 ATP* ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 8.80 Å
7YFN Core module of the NuA4 complex in S. cerevisiae Deposited 2022-07-08	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain T 1–3744（3744 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8ESC Structure of the Yeast NuA4 Histone Acetyltransferase Complex Deposited 2022-10-13	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain Z 1–3744（3744 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TRA1_YEAST
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain T； PDBConstruct 1–3744； UniProt 1–3744

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	7yfp
Deposition date deposition_date	2022-07-08
Structure title title	The NuA4 histone acetyltransferase complex from S. cerevisiae
Keywords keywords	histone acetyltransferase, H4, acetylation, NuA4, nucleosome, TRANSFERASE; TRANSFERASE
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	70.97 Å
Radius of gyration Rg (electron density) rg_electron	71.25 Å
Forward intensity I(0) i0	4372260000.00
Molecular weight molecular_weight	580650.0 kDa
Excluded volume excluded_volume	735570 Å³
Envelope volume envelope_volume	1178400 Å³
Hydration-shell volume shell_volume	143220 Å³
Envelope diameter envelope_diameter	238.9 Å
Shell Rg shell_rg	66.63 Å
Envelope Rg envelope_rg	69.33 Å
Shape Rg shape_rg	71.25 Å
Total Rg total_rg	71.20 Å
Total atoms total_atoms	40949
Residues n_residues	5028
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	263.7 Å
Rg (real space) rg_real	71.27 Å
Rg uncertainty (real space) rg_real_error	2.92 Å
I(0) (real space) i0_real	4.3740e+09
I(0) uncertainty (real space) i0_real_error	1.0690e+08
Rg (reciprocal space) rg_reciprocal	70.23 Å
I(0) (reciprocal space) i0_reciprocal	4364000000.0000
Solution quality estimate total_estimate	0.8493
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	71.9 Å
Skewness Skewness skewness	0.406
Kurtosis Kurtosis kurtosis	-0.425
Angular range angular_range	— – 0.1100 Å⁻¹
Current regularization parameter α current_alpha	0.0188
Highest regularization parameter α highest_alpha	311700000.0000
Real-space data points n_real_points	23
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.737; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.825

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Actin
Molecular weight formula_weight	41402.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	40949

EVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQEYDESGPSIVHHKCF

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Saccharomyces cerevisiae

Entity 2 Entity 2 polymer

Description description	ARP4 isoform 1
Molecular weight formula_weight	54021.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

VYGGDEVSAVVIDPGSYTTNIGYSGSDFPQSILPSVYGKYTADEGNKKIFSEQSIGIPRKDYELKPIIENGLVIDWDTAQEQWQWALQNELYLNSNSGIPALLTEPVWNSTENRKKSLEVLLEGMQFEACYLAPTSTCVSFAAGRPNCLVVDIGHDTCSVSPIVDGMTLSKSTRRNFIAGKFINHLIKKALEPKEIIPLFAIKQRKPEFIKKTFDYEVDKSLYDYANNRGFFQECKETLCHICPTKTLEETKTELSSTAKRSIESPWNEEIVFDNETRYGFAEELFLPKEDDIPANWPRSNSGVVKTWRNDYVPLKRTKPSGVNKSDKKVTPTEEKEQEAVSKSTSPAANSADTPNETGKRPLEEEKPPKENNELIGLADLVYSSIMSSDVDLRATLAHNVVLTGGTSSIPGLSDRLMTELNKILPSLKFRILTTGHTIERQYQSWLGGSILTSLGTFHQLWVGKKEYEEVGVERLLNDRF

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Saccharomyces cerevisiae

Entity 3 Entity 3 polymer

Description description	Chromatin modification-related protein EAF1
Molecular weight formula_weight	112667.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

MSSRPSSAVPNSASLSEDQSSDRSKFPKADDLIDERDRKLTELYCVSRLNQLLELTDENKLRKEIDAFLKKNDIRRGIRFDEASLPKLLHTAATPITKKKLKDVNLINVPNQRLSDSKMSRELPENSENVSVKSESHFVPSHDNSIRENMMDSLRPAEKTGGMWNKRPLESTMGGEEERHEKRQKMQSQSLESSNNSEMASLPISPRPPVPNALAHYTYYENIEYPPADPTEVQPAVKFKDPLIKNIMAKEIDTSDHYNENNVDALETVFLLMNDYIPSKIPQALPLAELKYMSQTLPLINLIPRAHKALTTNIINNALNEARITVVGSRIEELRRLGLWSLRQPKRFIDPWKQHNTHQNILLEEAKWMQADFKEGHKYKVAICTAMAQAIKDYWTYGEICCVKRKTLLPGKENKLSDDGRISEKSGRPSDTSRNDSDISIAGKDDIGIIANVDDITEKESAAANDNDENGKNEAGAKSDFDFADGLLSQEGAHDQIISSIDTKLLLKKPSSSSEVVLIQHEVAASSALIETEESKKELAPPFKLSIFVDELNTFEKTLIQDLPLYNGINEERPKKDDSLPFIPISKSVVSLDDNGFYKLLERQLIDEEPSISQLSKRRGMFYGNRRNHYLRPPAVPSLRYLQNRTPTIWLSEDDQELVKNINTYGYNWELISAHMTHRLTYSYLSNIERRTPWQCFERFVQLNERFNFSDLKGPRAHSAQQWLIEAHKFQQRQNRRISPLGVNTESIQRGHRRLRWASMFEAIRKCMKKRENTPRPNPTQPRKPLDCKNMKVPTPAEMSLLKAQRDEALRRDIQLRRTVKNRLQQRQQQSQQAHSSRAQSPIPSNGKSSSNLARNGQASAPRPNQKQYTEQDIIESYSRKLLEQKPDIGPEMALKAAKNYYRTLREQQQQLKQHQIQQQRQQLQEESSHVQQLQQLQPGSQAPPPKSSPSQSSLSNISNINSAPRIKSPTPQEILQRFQKQ

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Saccharomyces cerevisiae

Entity 4 Entity 4 polymer

Description description	SWR1-complex protein 4
Molecular weight formula_weight	55297.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

MSSSDIFDVLNIKQKSRSPTNGQVSVPSSSAANRPKPQVTGMQRELFNLLGENQPPVVIKSGNNFKEKMLSTSKPSPWSFVEFKANNSVTLRHWVKGSKELIGDTPKESPYSKFNQHLSIPSFTKEEYEAFMNENEGTQKSVESEKNHNENFTNEKKDESKNSWSFEEIEYLFNLCKKYDLRWFLIFDRYSYNNSRTLEDLKEKFYYTCRNYFKASDPSNPLLSSLNFSAEKEIERKKYLQRLLSRSAAEIAEEEALVVESKKFEMAAKRTLAERESLLRLLDSPHSDQTITQYLTSQGMSQLYNALLADKTRKRKHDLNIPENPWMKQQQQFAQHRQLQQLNVKKSEVKENLSPKKTKRQRQEMQTALKRKSESAYAEQLLKDFNSDERKALGVITHGEKLSPGVYLRSTKLSTFKPALQNKILAILQELSLPSRPVMPSFDVMERQEELLKKINTLIDLKKHVDKYEAGMSITK

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Saccharomyces cerevisiae

Entity 5 Entity 5 polymer

Description description	Enhancer of polycomb-like protein 1
Molecular weight formula_weight	96889.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F

MPTPSNAIEINDGSHKSGRSTRRSGSRSAHDDGLDSFSKGDSGAGASAGSSNSRFRHRKISVKQHLKIYLPNDLKHLDKDELQQREVVEIETGVEKNEEKEVHLHRILQMGSGHTKHKDYIPTPDASMTWNEYDKFYTGSFQETTSYIKFSATVEDCCGTNYNMDERDETFLNEQVNKGSSDILTEDEFEILCSSFEHAIHERQPFLSMDPESILSFEELKPTLIKSDMADFNLRNQLNHEINSHKTHFITQFDPVSQMNTRPLIQLIEKFGSKIYDYWRERKIEVNGYEIFPQLKFERPGEKEEIDPYVCFRRREVRHPRKTRRIDILNSQRLRALHQELKNAKDLALLVAKRENVSLNWINDELKIFDQRVKIKNLKRSLNISGEDDDLINHKRKRPTIVTVEQREAELRKAELKRAAAAAAAAKAKNNKRNNQLEDKSSRLTKQQQQQLLQQQQQQQQNALKTENGKQLANASSSSTSQPITSHVYVKLPSSKIPDIVLEDVDALLNSKEKNARKFVQEKMEKRKIEDADVFFNLTDDPFNPVFDMSLPKNFSTSNVPFASIASSKFQIDRSFYSSHLPEYLKGISDDIRIYDSNGRSRNKDNYNLDTKRIKKTELYDPFQENLEIHSREYPIKFRKRVGRSNIKYVDRMPNFTTSSTKSACSLMDFVDFDSIEKEQYSREGSNDTDSINVYDSKYDEFVRLYDKWKYDSPQNEYGIKFSDEPARLNQISNDTQVIRFGTMLGTKSYEQLREATIKYRRDYITRLKQKHIQHLQQQQQQQQQQQQQAQQQKQKSQNNNSNSSNSLKKLNDSLINSEAKQNSSITQKNSS

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Saccharomyces cerevisiae

Entity 6 Entity 6 polymer

Description description	Transcription-associated protein 1
Molecular weight formula_weight	433677.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	T

MSLTEQIEQFASRFRDDDATLQSRYSTLSELYDIMELLNSPEDYHFFLQAVIPLLLNQLKEVPISYDAHSPEQKLRNSMLDIFNRCLMNQTFQPYAMEVLEFLLSVLPKENEENGILCMKVLTTLFKSFKSILQDKLDSFIRIIIQIYKNTPNLINQTFYEAGKAEQGDLDSPKEPQADELLDEFSKNDEEKDFPSKQSSTEPRFENSTSSNGLRSSMFSFKILSECPITMVTLYSSYKQLTSTSLPEFTPLIMNLLNIQIKQQQEAREQAESRGEHFTSISTEIINRPAYCDFILAQIKATSFLAYVFIRGYAPEFLQDYVNFVPDLIIRLLQDCPSELSSARKELLHATRHILSTNYKKLFLPKLDYLFDERILIGNGFTMHETLRPLAYSTVADFIHNIRSELQLSEIEKTIKIYTGYLLDESLALTVQIMSAKLLLNLVERILKLGKENPQEAPRAKKLLMIIIDSYMNRFKTLNRQYDTIMKYYGRYETHKKEKAEKLKNSIQDNDKESEEFMRKVLEPSDDDHLMPQPKKEDINDSPDVEMTESDKVVKNDVEMFDIKNYAPILLLPTPTNDPIKDAFYLYRTLMSFLKTIIHDLKVFNPPPNEYTVANPKLWASVSRVFSYEEVIVFKDLFHECIIGLKFFKDHNEKLSPETTKKHFDISMPSLPVSATKDARELMDYLAFMFMQMDNATFNEIIEQELPFVYERMLEDSGLLHVAQSFLTSEITSPNFAGILLRFLKGKLKDLGNVDFNTSNVLIRLFKLSFMSVNLFPNINEVVLLPHLNDLILNSLKYSTTAEEPLVYFYLIRTLFRSIGGGRFENLYRSIKPILQVLLQSLNQMILTARLPHERELYVELCITVPVRLSVLAPYLPFLMKPLVFALQQYPDLVSQGLRTLELCIDNLTAEYFDPIIEPVIDDVSKALFNLLQPQPFNHAISHNVVRILGKLGGRNRQFLKPPTDLTEKTELDIDAIADFKINGMPEDVPLSVTPGIQSALNILQSYKSDIHYRKSAYKYLTCVLLLMTKSSAEFPTNYTELLKTAVNSIKLERIGIEKNFDLEPTVNKRDYSNQENLFLRLLESVFYATSIKELKDDAMDLLNNLLDHFCLLQVNTTLLNKRNYNGTFNIDLKNPNFMLDSSLILDAIPFALSYYIPEVREVGVLAYKRIYEKSCLIYGEELALSHSFIPELAKQFIHLCYDETYYNKRGGVLGIKVLIDNVKSSSVFLKKYQYNLANGLLFVLKDTQSEAPSAITDSAEKLLIDLLSITFADVKEEDLGNKVLENTLTDIVCELSNANPKVRNACQKSLHTISNLTGIPIVKLMDHSKQFLLSPIFAKPLRALPFTMQIGNVDAITFCLSLPNTFLTFNEELFRLLQESIVLADAEDESLSTNIQKTTEYSTSEQLVQLRIACIKLLAIALKNEEFATAQQGNIRIRILAVFFKTMLKTSPEIINTTYEALKGSLAENSKLPKELLQNGLKPLLMNLSDHQKLTVPGLDALSKLLELLIAYFKVEIGRKLLDHLTAWCRVEVLDTLFGQDLAEQMPTKIIVSIINIFHLLPPQADMFLNDLLLKVMLLERKLRLQLDSPFRTPLARYLNRFHNPVTEYFKKNMTLRQLVLFMCNIVQRPEAKELAEDFEKELDNFYDFYISNIPKNQVRVVSFFTNMVDLFNTMVITNGDEWLKKKGNMILKLKDMLNLTLKTIKENSFYIDHLQLNQSIAKFQALYLRFTELSERDQNPLLLDFIDFSFSNGIKASYSLKKFIFHNIIASSNKEKQNNFINDATLFVLSDKCLDARIFVLKNVINSTLIYEVATSGSLKSYLVEDKKPKWLELLHNKIWKNSNAILAYDVLDHHDLFRFELLQLSAIFIKADPEIIAEIKKDIIKFCWNFIKLEDTLIKQSAYLVTSYFISKFDFPIKVVTQVFVALLRSSHVEARYLVKQSLDVLTPVLHERMNAAGTPDTWINWVKRVMVENSSSQNNILYQFLISHPDLFFNSRDLFISNIIHHMNKITFMSNSNSDSHTLAIDLASLILYWENKTLEITNVNNTKTDSDGDVVMSDSKSDINPVEADTTAIIVDANNNSPISLHLREACTAFLIRYVCASNHRAIETELGLRAINILSELISDKHWTNVNVKLVYFEKFLIFQDLDSENILYYCMNALDVLYVFFKNKTKEWIMENLPTIQNLLEKCIKSDHHDVQEALQKVLQVIMKAIKAQGVSVIIEEESPGKTFIQMLTSVITQDLQETSSVTAGVTLAWVLFMNFPDNIVPLLTPLMKTFSKLCKDHLSISQPKDAMALEEARITTKLLEKVLYILSLKVSLLGDSRRPFLSTVALLIDHSMDQNFLRKIVNMSRSWIFNTEIFPTVKEKAAILTKMLAFEIRGEPSLSKLFYEIVLKLFDQEHFNNTEITVRMEQPFLVGTRVEDIGIRKRFMTILDNSLERDIKERLYYVIRDQNWEFIADYPWLNQALQLLYGSFNREKELSLKNIYCLSPPSILQEYLPENAEMVTEVNDLELSNFVKGHIASMQGLCRIISSDFIDSLIEIFYQDPKAIHRAWVTLFPQVYKSIPKNEKYGFVRSIITLLSKPYHTRQISSRTNVINMLLDSISKIESLELPPHLVKYLAISYNAWYQSINILESIQSNTSIDNTKIIEANEDALLELYVNLQEEDMFYGLWRRRAKYTETNIGLSYEQIGLWDKAQQLYEVAQVKARSGALPYSQSEYALWEDNWIQCAEKLQHWDVLTELAKHEGFTDLLLECGWRVADWNSDRDALEQSVKSVMDVPTPRRQMFKTFLALQNFAESRKGDQEVRKLCDEGIQLSLIKWVSLPIRYTPAHKWLLHGFQQYMEFLEATQIYANLHTTTVQNLDSKAQEIKRILQAWRDRLPNTWDDVNMWNDLVTWRQHAFQVINNAYLPLIPALQQSNSNSNINTHAYRGYHEIAWVINRFAHVARKHNMPDVCISQLARIYTLPNIEIQEAFLKLREQAKCHYQNMNELTTGLDVISNTNLVYFGTVQKAEFFTLKGMFLSKLRAYEEANQAFATAVQIDLNLAKAWAQWGFFNDRRLSEEPNNISFASNAISCYLQAAGLYKNSKIRELLCRILWLISIDDASGMLTNAFDSFRGEIPVWYWITFIPQLLTSLSHKEANMVRHILIRIAKSYPQALHFQLRTTKEDFAVIQRQTMAVMGDKPDTNDRNGRRQPWEYLQELNNILKTAYPLLALSLESLVAQINDRFKSTTDEDLFRLINVLLIDGTLNYNRLPFPRKNPKLPENTEKNLVKFSTTLLAPYIRPKFNADFIDNKPDYETYIKRLRYWRRRLENKLDRASKKENLEVLCPHLSNFHHQKFEDIEIPGQYLLNKDNNVHFIKIARFLPTVDFVRGTHSSYRRLMIRGHDGSVHSFAVQYPAVRHSRREERMFQLYRLFNKSLSKNVETRRRSIQFNLPIAIPLSPQVRIMNDSVSFTTLHEIHNEFCKKKGFDPDDIQDFMADKLNAAHDDALPAPDMTILKVEIFNSIQTMFVPSNVLKDHFTSLFTQFEDFWLFRKQFASQYSSFVFMSYMMMINNRTPHKIHVDKTSGNVFTLEMLPSRFPYERVKPLLKNHDLSLPPDSPIFHNNEPVPFRLTPNIQSLIGDSALEGIFAVNLFTISRALIEPDNELNTYLALFIRDEIISWFSNLHRPIIENPQLREMVQTNVDLIIRKVAQLGHLNSTPTVTTQFILDCIGSAVSPRNLARTDVNFMPWF

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Saccharomyces cerevisiae

Entity 7 Entity 7 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	7yfpA01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	4.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	197044

fit	/app/data/saxs_computation/yf/7yfp/7yfp.fit
pddf	/app/data/pr_computation/yf/7yfp/7yfp.pr.out
profile	/app/data/saxs_computation/yf/7yfp/7yfp.dat

The NuA4 histone acetyltransferase complex from S. cerevisiae

1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin

State in the Current Structure

Other States of the Same Protein in the Database

ARP4 isoform 1

State in the Current Structure

Other States of the Same Protein in the Database

Chromatin modification-related protein EAF1

State in the Current Structure

Other States of the Same Protein in the Database

SWR1-complex protein 4

State in the Current Structure

Other States of the Same Protein in the Database

Enhancer of polycomb-like protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Transcription-associated protein 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 polymer

Polymer Polymer

来源 Source

Entity 6 Entity 6 polymer

Polymer Polymer

来源 Source

Entity 7 Entity 7 non-polymer

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)