8rtt

Structure of the formin Cdc12 bound to the barbed end of phalloidin-stabilized F-actin.

Method: ELECTRON MICROSCOPY D_max: 170.2 Å Quality: REASONABLE

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

Actin, cytoplasmic 1, N-terminally processed

Homo sapiens

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 × 9 PDB declaration: nonameric（9） Consistent with protein copy count	Chain A； UniProt 1–375 Chain B； UniProt 1–375 Chain C； UniProt 1–375 Chain D； UniProt 1–375	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	Cell division control protein 12 × 2 （Q10059） Phalloidin × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 PO4 PHOSPHATE ION × 3	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP) cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE；3 seconds, force 0.	Resolution 3.56 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 8RTT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
21VV Cryo-EM structure of ncBAF bound to the nucleosome Deposited 2025-12-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 14-meric	Chain J 1–375（375 aa）	Not recorded	BEF BERYLLIUM TRIFLUORIDE ION × 1 MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8；20 mM HEPES pH 8.0, 100 mM KCl, 2 mM MgCl2, 2 mM DTT, 0.5 mM ADP, 8 mM NaF, 1 mM BeSO4. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.70 Å
3D2U Structure of UL18, a Peptide-Binding Viral MHC Mimic, Bound to a Host Inhibitory Receptor Deposited 2008-05-08	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 C 170–178（9 aa） Fragment：sequence database residues 170-178	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 MAN alpha-D-mannopyranose × 1 BMA beta-D-mannopyranose × 1 FUC alpha-L-fucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；0.4 M Mg(NO3)2, and 16~22% (w/v) PEG 33500, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.21 Å R-free 0.259
3D2U Structure of UL18, a Peptide-Binding Viral MHC Mimic, Bound to a Host Inhibitory Receptor Deposited 2008-05-08	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 G 170–178（9 aa） Fragment：sequence database residues 170-178	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；0.4 M Mg(NO3)2, and 16~22% (w/v) PEG 33500, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.21 Å R-free 0.259
3J82 Electron cryo-microscopy of DNGR-1 in complex with F-actin Deposited 2014-09-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.70 Å
3LUE Model of alpha-actinin CH1 bound to F-actin Deposited 2010-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa） Chain F 2–375（374 aa） Chain G 2–375（374 aa） Chain H 2–375（374 aa） Chain I 2–375（374 aa） Chain J 2–375（374 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM vitrification conditions Cryogen ETHANE	Resolution 15.00 Å
6ANU Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain Deposited 2017-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	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） Chain F 1–375（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.00 Å
6ICT Structure of SETD3 bound to SAH and methylated actin Deposited 2018-09-07	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 E 66–88（23 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Magnesium acetate tetrahydrate 0.1M Sodium cacodylate trihydrate pH 6.5 20% Polyethylene glycol 8000	Resolution 1.95 Å R-free 0.214
6ICT Structure of SETD3 bound to SAH and methylated actin Deposited 2018-09-07	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 × 2 PDB declaration: dimeric	Chain G 66–88（23 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Magnesium acetate tetrahydrate 0.1M Sodium cacodylate trihydrate pH 6.5 20% Polyethylene glycol 8000	Resolution 1.95 Å R-free 0.214
6ICT Structure of SETD3 bound to SAH and methylated actin Deposited 2018-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 66–88（23 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Magnesium acetate tetrahydrate 0.1M Sodium cacodylate trihydrate pH 6.5 20% Polyethylene glycol 8000	Resolution 1.95 Å R-free 0.214
6ICT Structure of SETD3 bound to SAH and methylated actin Deposited 2018-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 66–88（23 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Magnesium acetate tetrahydrate 0.1M Sodium cacodylate trihydrate pH 6.5 20% Polyethylene glycol 8000	Resolution 1.95 Å R-free 0.214
6ICV Structure of SETD3 bound to SAH and unmodified actin Deposited 2018-09-07	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 C 66–88（23 aa）	Not recorded	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M HEPES sodium pH 7.5 2% Polyethylene glycol 400 2.0M Ammonium sulfate	Resolution 2.15 Å R-free 0.205
6ICV Structure of SETD3 bound to SAH and unmodified actin Deposited 2018-09-07	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 × 2 PDB declaration: dimeric	Chain D 66–88（23 aa）	Not recorded	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M HEPES sodium pH 7.5 2% Polyethylene glycol 400 2.0M Ammonium sulfate	Resolution 2.15 Å R-free 0.205
6LTJ Structure of nucleosome-bound human BAF complex Deposited 2020-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 18 PDB declaration: eicosameric	Chain K 1–375（375 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
6MBJ SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, P21 Crystal Form Deposited 2018-08-30	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 Y 66–80（15 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 19 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 3 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；292 K；0.2 M Ammonium acetate, 0.1 M Sodium citrate tribasic dihydrate pH 5.6, 30% w/v Polyethylene glycol 4,000	Resolution 1.78 Å R-free 0.223
6MBJ SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, P21 Crystal Form Deposited 2018-08-30	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 × 2 PDB declaration: dimeric	Chain Z 66–80（15 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 16 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；292 K；0.2 M Ammonium acetate, 0.1 M Sodium citrate tribasic dihydrate pH 5.6, 30% w/v Polyethylene glycol 4,000	Resolution 1.78 Å R-free 0.223
6MBK SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, First P212121 Crystal Form Deposited 2018-08-30	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 Y 66–80（15 aa） Fragment：residues 66-80	Not recorded	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 6 GOL GLYCEROL × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；0.2 M Ammonium sulfate, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350	Resolution 1.69 Å R-free 0.243
6MBK SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, First P212121 Crystal Form Deposited 2018-08-30	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 × 2 PDB declaration: dimeric	Chain Z 66–80（15 aa） Fragment：residues 66-80	Not recorded	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 8 GOL GLYCEROL × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；0.2 M Ammonium sulfate, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350	Resolution 1.69 Å R-free 0.243
6MBL SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, Second P212121 Crystal Form Deposited 2018-08-30	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 Y 66–80（15 aa） Fragment：residues 66-80	Not recorded	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；0.2 M Sodium chloride, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350	Resolution 2.20 Å R-free 0.227
6NBW Ternary Complex of Beta/Gamma-Actin with Profilin and AnCoA-NAA80 Deposited 2018-12-10	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 × 3 PDB declaration: trimeric	Chain A 2–375（374 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 LAB LATRUNCULIN B × 1 GOL GLYCEROL × 2 SOP [(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL (3R)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-{[3-OXO-3-({2-[(2-OXOPROPYL)THIO]ETHYL}AMINO)PROPYL]AMINO}BUTYL DIHYDROGEN DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；15% PEG 3350, 50mM MES pH6.2, 50mM NH4NO3	Resolution 2.50 Å R-free 0.209
6OX0 SETD3 in Complex with an Actin Peptide with Sinefungin Replacing SAH as Cofactor Deposited 2019-05-13	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 Y 66–80（15 aa） Fragment：residues 66-80	Not recorded	SFG SINEFUNGIN × 1 EDO 1,2-ETHANEDIOL × 18	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 1.75 Å R-free 0.225
6OX0 SETD3 in Complex with an Actin Peptide with Sinefungin Replacing SAH as Cofactor Deposited 2019-05-13	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 × 2 PDB declaration: dimeric	Chain Z 66–80（15 aa） Fragment：residues 66-80	Not recorded	SFG SINEFUNGIN × 1 EDO 1,2-ETHANEDIOL × 11	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 1.75 Å R-free 0.225
6OX1 SETD3 in Complex with an Actin Peptide with Target Histidine Partially Methylated Deposited 2019-05-13	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 Y 66–80（15 aa） Fragment：residues 66-80	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 EDO 1,2-ETHANEDIOL × 15	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 1.95 Å R-free 0.201
6OX1 SETD3 in Complex with an Actin Peptide with Target Histidine Partially Methylated Deposited 2019-05-13	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 × 2 PDB declaration: dimeric	Chain Z 66–80（15 aa） Fragment：residues 66-80	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 1.95 Å R-free 0.201
6OX2 SETD3in Complex with an Actin Peptide with the Target Histidine Fully Methylated Deposited 2019-05-13	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 Y 66–80（15 aa） Fragment：residues 66-80	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 15	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 2.09 Å R-free 0.239
6OX2 SETD3in Complex with an Actin Peptide with the Target Histidine Fully Methylated Deposited 2019-05-13	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 × 2 PDB declaration: dimeric	Chain Z 66–80（15 aa） Fragment：residues 66-80	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 8 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 2.09 Å R-free 0.239
6OX4 A SETD3 Mutant (N255A) in Complex with an Actin Peptide Deposited 2019-05-13	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 Y 66–80（15 aa） Fragment：residues 66-80	Not recorded	EDO 1,2-ETHANEDIOL × 17 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 3 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 2.29 Å R-free 0.236
6OX4 A SETD3 Mutant (N255A) in Complex with an Actin Peptide Deposited 2019-05-13	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 × 2 PDB declaration: dimeric	Chain Z 66–80（15 aa） Fragment：residues 66-80	Not recorded	EDO 1,2-ETHANEDIOL × 15 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 2.29 Å R-free 0.236
6OX5 A SETD3 Mutant (N255A) in Complex with an Actin Peptide with His73 Replaced with Lysine Deposited 2019-05-13	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 Y 66–83（18 aa）	Mutation：H73K	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000	Resolution 2.10 Å R-free 0.205
7AS4 Recombinant human gTuRC Deposited 2020-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 33 PDB declaration: 33-meric	Chain 7 2–375（374 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 14	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.13 Å
7P1H Structure of the V. vulnificus ExoY-G-actin-profilin complex Deposited 2021-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 4–375（372 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
7VDV The overall structure of human chromatin remodeling PBAF-nucleosome complex Deposited 2021-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 22 PDB declaration: 24-meric	Chain P 1–375（375 aa）	Not recorded	BEF BERYLLIUM TRIFLUORIDE ION × 1 MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7W28 Crystal Structure of SETD3-SAH in complex with betaA-4PyrAla73 peptide Deposited 2021-11-22	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 P 66–81（16 aa） Fragment：SAH	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；289 K；30%(w/v) PEG4000, 0.1 M Tris base/Hydrochloric acid 8.5, 0.2M Lithium sulfate.	Resolution 1.79 Å R-free 0.211
7W29 Crystal Structure of SETD3-SAH in complex with betaA-Orn73 peptide Deposited 2021-11-23	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 P 66–81（16 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；289 K；20%(w/v) PEG6000, 0.1M Bicine/Sodium hydroxide 9.0	Resolution 2.90 Å R-free 0.279
8COG Human arginylated beta-actin Deposited 2023-02-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 2–375（374 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；Actin for EM was polymerized by mixing, 20 ul 20 uM G-actin, 8 ul 10x MKE and 52 ul 5 mM HEPES-KOH pH 7.4 containing 0.2 mM ATP and 0.5 mM DTT and incubating at RT for 1 hour. cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.50 Å
8DNH Cryo-EM structure of nonmuscle beta-actin Deposited 2022-07-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
8OI8 Cryo-EM structure of ADP-bound, filamentous beta-actin harboring the R183W mutation Deposited 2023-03-22	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）	Mutation：R183W, C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R183W, C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R183W, C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R183W, C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R183W, C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1x KMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA) supplemented with 0.02% Tween20 (v/v) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.28 Å
8OID Cryo-EM structure of ADP-bound, filamentous beta-actin harboring the N111S mutation Deposited 2023-03-22	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）	Mutation：N111S, C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N111S, C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N111S, C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N111S, C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N111S, C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1x KMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA) supplemented with 0.02% Tween20 (v/v) cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.30 Å
8QR1 Cryo-EM structure of the human Tip60 complex Deposited 2023-10-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: 13-meric	Chain B 1–375（375 aa） 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 2.40 Å
8RTY Structure of the F-actin barbed end bound by Cdc12 and profilin (ring complex) at a resolution of 6.3 Angstrom Deposited 2024-01-29	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 10 PDB declaration: decameric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 PO4 PHOSPHATE ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP) cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3 seconds, force 0.	Resolution 6.25 Å
8RU2 Structure of the F-actin barbed end bound by formin mDia1 Deposited 2024-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3 seconds, force 0.	Resolution 3.49 Å
8VRD Rigid body fitted model for free recombinant gamma tubulin ring complex. Deposited 2024-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric	Chain S 1–375（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.00 Å
8VRJ Rigid body fitted model for gamma tubulin ring complex capped microtubule Deposited 2024-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric	Chain 9 1–375（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.70 Å
8VRK Rigid body fitted model for refined density map of gamma tubulin ring complex capped microtubule Deposited 2024-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric	Chain 9 1–375（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.50 Å
8X15 Structure of nucleosome-bound SRCAP-C in the apo state Deposited 2023-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 23 PDB declaration: 25-meric	Chain S 1–375（375 aa） Chain U 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8X19 Structure of nucleosome-bound SRCAP-C in the ADP-BeFx-bound state Deposited 2023-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 23 PDB declaration: 25-meric	Chain S 1–375（375 aa） Chain U 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8X1C Structure of nucleosome-bound SRCAP-C in the ADP-bound state Deposited 2023-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 23 PDB declaration: 25-meric	Chain S 1–375（375 aa） Chain U 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8XVT The core subcomplex of human NuA4/TIP60 complex Deposited 2024-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric	Chain K 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9B2Z Actin-bound Legionella pneumophila AMPylase LnaB with AMPylated catalytic histidine Deposited 2024-03-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–375（375 aa）	Not recorded	AMP ADENOSINE MONOPHOSPHATE × 1 CA CALCIUM ION × 1 LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.83 Å
9B7J Cryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1 Deposited 2024-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.49 Å
9B85 Cryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1 Deposited 2024-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 19 PDB declaration: 19-meric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 8 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.47 Å
9C57 Reconstituted P400 Subcomplex of the human TIP60 complex Deposited 2024-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric	Chain J 1–375（375 aa）	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.75 Å
9C62 P400 subcomplex of the native human TIP60 complex Deposited 2024-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain J 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.28 Å
9C6N ARP module of the human TIP60 complex Deposited 2024-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain J 1–375（375 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.29 Å
9CAC Cryo-EM structure of the RuvBL lobe of the native human TIP60 complex (composite structure) Deposited 2024-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: 13-meric	Chain K 1–375（375 aa） Chain L 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.43 Å
9CAE Cryo-EM structure of the reconstituted RuvBL lobe of the human TIP60 complex (composite structure) Deposited 2024-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain L 1–375（375 aa）	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å
9FJM Cryo-EM structure of the phalloidin-bound pointed end of the actin filament. Deposited 2024-05-31	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 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 PO4 PHOSPHATE ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP) cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3 seconds, force 0.	Resolution 3.65 Å
9GXI Subtomogram average of fascin-actin complex Deposited 2024-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain B 1–375（375 aa） Chain C 1–375（375 aa） Chain D 1–375（375 aa） Chain E 1–375（375 aa） Chain F 1–375（375 aa） Chain G 1–375（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.00 Å
9I8G Inwards conformation' of the human gamma-TuRC from purified centrosomes obtained by rigid body docking Deposited 2025-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 33 PDB declaration: 33-meric	Chain U 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 14	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 22.40 Å
9I8H Outwards conformation' of the human gamma-TuRC from purified centrosomes obtained by rigid body docking Deposited 2025-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 33 PDB declaration: 33-meric	Chain U 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 14	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 23.20 Å
9P1I Atomic structure of vibrio effector fragment VopV bound to Beta-cytoplasmic/gamma1-cytoplasmic F-actin Deposited 2025-06-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain Q 1–375（375 aa） Chain R 1–375（375 aa） Chain S 1–375（375 aa） Chain T 1–375（375 aa） Chain U 1–375（375 aa） Chain V 1–375（375 aa） Chain W 1–375（375 aa） Chain X 1–375（375 aa） Chain Y 1–375（375 aa） Chain Z 1–375（375 aa） Chain a 1–375（375 aa） Chain b 1–375（375 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 12 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9QEW Cryo-EM structure of the undecorated actin filament in the ADP-Pi state. Deposited 2025-03-11	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 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 PO4 PHOSPHATE ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.01% Tween20). cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.18 Å
9QEY Cryo-EM structure of the actin filament bound by a single Coronin-1B molecule. Deposited 2025-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 PO4 PHOSPHATE ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.01% Tween20). cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.74 Å
9QF2 Cryo-EM structure of the fully Coronin-1B-decorated actin filament in the ADP state. Deposited 2025-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 10 PDB declaration: decameric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.01% Tween20). cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.42 Å
9QFB Cryo-EM structure of the fully Coronin-1B-decorated actin filament in the ADP state. Deposited 2025-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 14 PDB declaration: 14-meric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa） Chain F 2–375（374 aa） Chain G 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.01% Tween20). cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.74 Å
9QFD Cryo-EM structure of the fully cofilin-1-decorated actin filament (cofilactin) Deposited 2025-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa） Chain F 2–375（374 aa） Chain G 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20). cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.61 Å
9QFE Cryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands Deposited 2025-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 14 PDB declaration: 14-meric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa） Chain F 2–375（374 aa） Chain G 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20). cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.12 Å
9QFG Cryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1, strand boundary Deposited 2025-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 14 PDB declaration: 14-meric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa） Chain F 2–375（374 aa） Chain G 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20). cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.49 Å
9QFJ Cryo-EM structure of the cofilactin filament core at 2.3 Angstrom resolution. Deposited 2025-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.015% Tween) cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.31 Å
9QFK Cryo-EM structure of the Coronin-1B-decorated actin filament bound by one Cofilin-1 molecule (crosslinked) Deposited 2025-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 14 PDB declaration: 14-meric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa） Chain F 2–375（374 aa） Chain G 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20). cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.99 Å
9QFO Cryo-EM structure of the cofilactin filament pointed end Deposited 2025-03-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa） Chain F 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.015% Tween20) cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.96 Å
9QFQ Cryo-EM structure of the cofilactin barbed end bound by AIP1 Deposited 2025-03-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 11 PDB declaration: 11-meric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.015% Tween20) cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.76 Å
9QFW Cryo-EM structure of the cofilactin barbed end bound by two AIP1 molecules Deposited 2025-03-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 12 PDB declaration: 12-meric	Chain A 2–375（374 aa） Chain B 2–375（374 aa） Chain C 2–375（374 aa） Chain D 2–375（374 aa） Chain E 2–375（374 aa）	Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C272A Non-standard monomer：Yes (specific site not provided by mmCIF)	MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.015% Tween20) cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.16 Å
9QVM Cryo-EM reconstruction of the NEDD1 anchor protein and CDK5RAP2 bound to the gamma-tubulin ring complex Deposited 2025-04-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain Z 1–375（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 6.80 Å
9QVN Cryo-EM reconstruction of the NEDD1 anchor protein bound to the gamma-tubulin ring complex Deposited 2025-04-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 45 PDB declaration: 45-meric	Chain Z 1–375（375 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.70 Å
9RL4 Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL-6 Deposited 2025-06-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 20 PDB declaration: 22-meric	Chain K 1–375（375 aa）	Not recorded	PTD PENTANEDIAL × 16 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9RMC Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL+6 class 1 Deposited 2025-06-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 20 PDB declaration: 22-meric	Chain K 1–375（375 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
9RN1 Structure of BAF-nucleosome complex with OCT4-SOX2 at SHL+6 in ADP-bound state, BAF47 bound to ATPase lobe 2 Deposited 2025-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 20 PDB declaration: 22-meric	Chain K 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 5.90 Å
9RN2 Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL+6 class 2 Deposited 2025-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 19 PDB declaration: 21-meric	Chain K 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 4.10 Å
9UXA local ARP-NCP structure of the ncBAF-nucleosome complex in the apo state Deposited 2025-05-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 14-meric	Chain I 2–375（374 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.28 Å
9UXB The apo structure of BCL7B-containing ARP module of the human SWI/SNF complex Deposited 2025-05-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 2–375（374 aa）	Not recorded	MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.92 Å
9UXC The ADP-bound structure of BCL7B-containing ARP module of the human SWI/SNF complex Deposited 2025-05-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 2–375（374 aa）	Not recorded	MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.74 Å
9WBZ The structure of NCP-motor-ARP module of ncBAF-nucleosome complex Deposited 2025-08-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: tetradecameric	Chain L 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 2.90 Å
9WC1 The structure of ARP module in ncBAF complex Deposited 2025-08-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 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 3.40 Å

72 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACTB_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–375； UniProt 1–375 Author chain B； PDBConstruct 1–375； UniProt 1–375 Author chain C； PDBConstruct 1–375； UniProt 1–375 Author chain D； PDBConstruct 1–375； UniProt 1–375

Cell division control protein 12

Schizosaccharomyces pombe

UniProt Q10059

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 × 9 PDB declaration: nonameric（9） Consistent with protein copy count	Chain E； UniProt 972–1390 Chain F； UniProt 972–1390	Not recorded	Actin, cytoplasmic 1, N-terminally processed × 4 （P60709） Phalloidin × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 PO4 PHOSPHATE ION × 3	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP) cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE；3 seconds, force 0.	Resolution 3.56 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8RTT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8RTY Structure of the F-actin barbed end bound by Cdc12 and profilin (ring complex) at a resolution of 6.3 Angstrom Deposited 2024-01-29	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 10 PDB declaration: decameric	Chain E 881–1390（510 aa） Chain F 881–1390（510 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 PO4 PHOSPHATE ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP) cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3 seconds, force 0.	Resolution 6.25 Å

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

View Construct and Data Evidence

UniProt name	CDC12_SCHPO
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–419； UniProt 972–1390 Author chain F； PDBConstruct 1–419； UniProt 972–1390

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8rtt
Deposition date deposition_date	2024-01-29
Structure title title	Structure of the formin Cdc12 bound to the barbed end of phalloidin-stabilized F-actin.
Keywords keywords	actin, formin, Cdc12, actin assembly., STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
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	49.55 Å
Radius of gyration Rg (electron density) rg_electron	49.51 Å
Forward intensity I(0) i0	990030000.00
Molecular weight molecular_weight	258830.0 kDa
Excluded volume excluded_volume	323040 Å³
Envelope volume envelope_volume	458130 Å³
Hydration-shell volume shell_volume	79528 Å³
Envelope diameter envelope_diameter	178.3 Å
Shell Rg shell_rg	51.09 Å
Envelope Rg envelope_rg	48.81 Å
Shape Rg shape_rg	49.54 Å
Total Rg total_rg	49.48 Å
Total atoms total_atoms	18155
Residues n_residues	2264
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	170.2 Å
Rg (real space) rg_real	49.67 Å
Rg uncertainty (real space) rg_real_error	1.79 Å
I(0) (real space) i0_real	9.9000e+08
I(0) uncertainty (real space) i0_real_error	2.1550e+07
Rg (reciprocal space) rg_reciprocal	49.55 Å
I(0) (reciprocal space) i0_reciprocal	989900000.0000
Solution quality estimate total_estimate	0.6605
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	58.5 Å
Skewness Skewness skewness	0.381
Kurtosis Kurtosis kurtosis	-0.317
Angular range angular_range	— – 0.1600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	69220000.0000
Real-space data points n_real_points	33
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 0.087; Positv: 1.000; Valcen: 0.991; Smooth: 0.767

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Actin, cytoplasmic 1, N-terminally processed
Molecular weight formula_weight	41763.6 kDa
Mutation mutation	C272A
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	18155

MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Trichoplusia ni

Entity 2 Entity 2 polymer

Description description	Cell division control protein 12
Molecular weight formula_weight	48495.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F

SKDDLHKTTGLTRRPTRRLKQMHWEKLNSGLEFTFWTGPSDEANKILETLHTSGVLDELDESFAMKEAKTLVKKTCARTDYMSSELQKLFGIHFHKLSHKNPNEIIRMILHCDDSMNECVEFLSSDKVLNQPKLKADLEPYRIDWANGGDLVNSEKDASELSRWDYLYVRLIVDLGGYWNQRMNALKVKNIIETNYENLVRQTKLIGRAALELRDSKVFKGLLYLILYLGNYMNDYVRQAKGFAIGSLQRLPLIKNANNTKSLLHILDITIRKHFPQFDNFSPELSTVTEAAKLNIEAIEQECSELIRGCQNLQIDCDSGALSDPTVFHPDDKILSVILPWLMEGTKKMDFLKEHLRTMNTTLNNAMRYFGEQPNDPNSKNLFFKRVDSFIIDYSKARSDNLKSEEEEASQHRRLNLVN

来源 Source

来源生物 organism	Schizosaccharomyces pombe
通用名 common_name	fission yeast
NCBI Class编号 ncbi_taxonomy_id	4896
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Phalloidin
Molecular weight formula_weight	808.9 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,I,J

WXATCPA

Entity 4 Entity 4 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	3

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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	triclinic

Resolution resolution	3.56 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	154570

fit	/app/data/saxs_computation/rt/8rtt/8rtt.fit
pddf	/app/data/pr_computation/rt/8rtt/8rtt.pr.out
profile	/app/data/saxs_computation/rt/8rtt/8rtt.dat

Structure of the formin Cdc12 bound to the barbed end of phalloidin-stabilized F-actin.

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

Actin, cytoplasmic 1, N-terminally processed

State in the Current Structure

Other States of the Same Protein in the Database

Cell division control protein 12

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 (6)

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

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)