7lny

Apo structure of the Histone chaperone ASF1A residues 1-155

Method: X-RAY DIFFRACTION D_max: 139.0 Å Quality: GOOD

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

Histone chaperone ASF1A

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–155	Fragment：Residues 1-155	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 ml reservoir of 22% PEG3350 and 6% of Tascimate pH6.0	Resolution 2.10 Å R-free 0.242
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 1–155	Fragment：Residues 1-155	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 ml reservoir of 22% PEG3350 and 6% of Tascimate pH6.0	Resolution 2.10 Å R-free 0.242
3	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain C； UniProt 1–155	Fragment：Residues 1-155	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 ml reservoir of 22% PEG3350 and 6% of Tascimate pH6.0	Resolution 2.10 Å R-free 0.242
4	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain D； UniProt 1–155	Fragment：Residues 1-155	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 ml reservoir of 22% PEG3350 and 6% of Tascimate pH6.0	Resolution 2.10 Å R-free 0.242
5	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain E； UniProt 1–155	Fragment：Residues 1-155	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 ml reservoir of 22% PEG3350 and 6% of Tascimate pH6.0	Resolution 2.10 Å R-free 0.242
6	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain F； UniProt 1–155	Fragment：Residues 1-155	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 ml reservoir of 22% PEG3350 and 6% of Tascimate pH6.0	Resolution 2.10 Å R-free 0.242
7	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain G； UniProt 1–155	Fragment：Residues 1-155	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；1 ml reservoir of 22% PEG3350 and 6% of Tascimate pH6.0	Resolution 2.10 Å R-free 0.242

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 7LNY	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1TEY NMR structure of human histone chaperone, ASF1A Deposited 2004-05-26	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–156（156 aa） Fragment：N-TERMINAL DOMAIN (residues 1-156)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 20 mM；Pressure ambient NMR sample composition 1mM Asf1A U-15N,13C; 20mM tris-D11; 1mM EDTA; 0.1mM DSS; 0.1 mM NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2I32 Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly Deposited 2006-08-17	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–157（157 aa） Fragment：Residues 1-157	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；CRYSTALS OF THE HUMAN ASF1AN-HIRA(425-472) COMPLEX WERE GROWN BY HANGING DROP VAPOR DIFFUSION AT ROOM TEMPERATURE AND WERE OBTAINED BY MIXING 2 UL OF A 0.5 MM PROTEIN COMPLEX SOLUTION (IN 20 MM HEPES PH 7.0, 150 MM NACL AND 5 MM BETA-ME) WITH 2 UL OF RESERVOIR SOLUTION CONTAINING 1.44 M NAH2PO4 AND 0.16 M K2HPO4 AT PH 5.6, AND EQUILIBRATING OVER 1.0 ML OF RESERVOIR SOLUTION. CRYSTALS WERE FULLY GROWN WITHIN TWO WEEKS TO A TYPICAL SIZE OF 0.3MMX0.3MMX0.2MM, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K	Resolution 2.70 Å R-free 0.269
2I32 Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly Deposited 2006-08-17	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–157（157 aa） Fragment：Residues 1-157	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；CRYSTALS OF THE HUMAN ASF1AN-HIRA(425-472) COMPLEX WERE GROWN BY HANGING DROP VAPOR DIFFUSION AT ROOM TEMPERATURE AND WERE OBTAINED BY MIXING 2 UL OF A 0.5 MM PROTEIN COMPLEX SOLUTION (IN 20 MM HEPES PH 7.0, 150 MM NACL AND 5 MM BETA-ME) WITH 2 UL OF RESERVOIR SOLUTION CONTAINING 1.44 M NAH2PO4 AND 0.16 M K2HPO4 AT PH 5.6, AND EQUILIBRATING OVER 1.0 ML OF RESERVOIR SOLUTION. CRYSTALS WERE FULLY GROWN WITHIN TWO WEEKS TO A TYPICAL SIZE OF 0.3MMX0.3MMX0.2MM, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K	Resolution 2.70 Å R-free 0.269
3AAD Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction Deposited 2009-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–155（155 aa） Fragment：Residues 1-155 Chain D 1–155（155 aa） Fragment：Residues 1-155	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.65；293 K；0.1M MES, 1.1M AMMONIUM SULFATE, 0.25M LITHIUM SULFATE, pH 5.65, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.30 Å R-free 0.293
5C3I Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2 Deposited 2015-06-17	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain I 1–175（175 aa） Fragment：UNP residues 1-175	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；20% PEG 3350, 2% Tacsimate,0.1 M Tris-HCl pH 8.0	Resolution 3.50 Å R-free 0.253
5C3I Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2 Deposited 2015-06-17	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–175（175 aa） Fragment：UNP residues 1-175	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；20% PEG 3350, 2% Tacsimate,0.1 M Tris-HCl pH 8.0	Resolution 3.50 Å R-free 0.253
5C3I Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2 Deposited 2015-06-17	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 1–175（175 aa） Fragment：UNP residues 1-175	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；20% PEG 3350, 2% Tacsimate,0.1 M Tris-HCl pH 8.0	Resolution 3.50 Å R-free 0.253
5C3I Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2 Deposited 2015-06-17	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain M 1–175（175 aa） Fragment：UNP residues 1-175	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；20% PEG 3350, 2% Tacsimate,0.1 M Tris-HCl pH 8.0	Resolution 3.50 Å R-free 0.253
5C3I Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2 Deposited 2015-06-17	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain Q 1–175（175 aa） Fragment：UNP residues 1-175	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；20% PEG 3350, 2% Tacsimate,0.1 M Tris-HCl pH 8.0	Resolution 3.50 Å R-free 0.253
5C3I Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2 Deposited 2015-06-17	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain U 1–175（175 aa） Fragment：UNP residues 1-175	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；20% PEG 3350, 2% Tacsimate,0.1 M Tris-HCl pH 8.0	Resolution 3.50 Å R-free 0.253
6F0F Crystal structure ASF1-ip2_s Deposited 2017-11-20	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–156（156 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7.5；298 K；Tris-HCl 0.1M pH7.5, PEG8000 5%	Resolution 2.00 Å R-free 0.227
6F0G Crystal structure ASF1-ip3 Deposited 2017-11-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–156（156 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Citrate 0.1M pH 2.5, LiSO4 0.25M, PEG8000 7%	Resolution 2.30 Å R-free 0.267
6F0G Crystal structure ASF1-ip3 Deposited 2017-11-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–156（156 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Citrate 0.1M pH 2.5, LiSO4 0.25M, PEG8000 7%	Resolution 2.30 Å R-free 0.267
6F0H Crystal structure ASF1-ip4 Deposited 2017-11-20	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 1–156（156 aa） Chain C 1–156（156 aa）	Not recorded	SO4 SULFATE ION × 12 GOL GLYCEROL × 6 CIT CITRIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Citrate 0.1M pH 2.5, LiSO4 0.5M, PEG8000 10%	Resolution 1.98 Å R-free 0.242
6ZUF Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone Deposited 2020-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–156（156 aa）	Not recorded	GOL GLYCEROL × 3 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；293 K；100 mM Sodium Citrate pH4.2, 300 mM LiSO4, 26% PEG3350	Resolution 1.80 Å R-free 0.210
6ZUF Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone Deposited 2020-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–156（156 aa）	Not recorded	GOL GLYCEROL × 6 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；293 K；100 mM Sodium Citrate pH4.2, 300 mM LiSO4, 26% PEG3350	Resolution 1.80 Å R-free 0.210
7LO0 Structure of human ASF1a in complex with a TLK2 peptide Deposited 2021-02-08	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–155（155 aa） Fragment：Residues 1-155	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose	Resolution 2.71 Å R-free 0.226
7LO0 Structure of human ASF1a in complex with a TLK2 peptide Deposited 2021-02-08	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–155（155 aa） Fragment：Residues 1-155	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose	Resolution 2.71 Å R-free 0.226
7LO0 Structure of human ASF1a in complex with a TLK2 peptide Deposited 2021-02-08	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–155（155 aa） Fragment：Residues 1-155	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose	Resolution 2.71 Å R-free 0.226
7LO0 Structure of human ASF1a in complex with a TLK2 peptide Deposited 2021-02-08	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 1–155（155 aa） Fragment：Residues 1-155	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose	Resolution 2.71 Å R-free 0.226
7LO0 Structure of human ASF1a in complex with a TLK2 peptide Deposited 2021-02-08	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–155（155 aa） Fragment：Residues 1-155	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose	Resolution 2.71 Å R-free 0.226
7LO0 Structure of human ASF1a in complex with a TLK2 peptide Deposited 2021-02-08	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 1–155（155 aa） Fragment：Residues 1-155	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose	Resolution 2.71 Å R-free 0.226
7LO0 Structure of human ASF1a in complex with a TLK2 peptide Deposited 2021-02-08	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 1–155（155 aa） Fragment：Residues 1-155	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose	Resolution 2.71 Å R-free 0.226
7LO0 Structure of human ASF1a in complex with a TLK2 peptide Deposited 2021-02-08	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 1–155（155 aa） Fragment：Residues 1-155	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose	Resolution 2.71 Å R-free 0.226
7V6Q Crystal structure of sNASP-ASF1A-H3.1-H4 complex Deposited 2021-08-20	Different construct 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 1–156（156 aa）	Not recorded	GOL GLYCEROL × 4 1PE PENTAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；18% (v/v) Tacsimate, pH 5.0 11% (v/v) PEG2000MME	Resolution 3.00 Å R-free 0.203
7V6Q Crystal structure of sNASP-ASF1A-H3.1-H4 complex Deposited 2021-08-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 1–156（156 aa）	Not recorded	GOL GLYCEROL × 2 1PE PENTAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；18% (v/v) Tacsimate, pH 5.0 11% (v/v) PEG2000MME	Resolution 3.00 Å R-free 0.203
8BV1 Peptide inhibitor P4 in complex with ASF1 histone chaperone Deposited 2022-12-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–156（156 aa）	Not recorded	GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290.15 K；0.1 M Tris pH 8.5 30% (w/v) PEG 400	Resolution 2.83 Å R-free 0.221
8BV1 Peptide inhibitor P4 in complex with ASF1 histone chaperone Deposited 2022-12-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–156（156 aa）	Not recorded	GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290.15 K；0.1 M Tris pH 8.5 30% (w/v) PEG 400	Resolution 2.83 Å R-free 0.221
8BV1 Peptide inhibitor P4 in complex with ASF1 histone chaperone Deposited 2022-12-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–156（156 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290.15 K；0.1 M Tris pH 8.5 30% (w/v) PEG 400	Resolution 2.83 Å R-free 0.221
8BV1 Peptide inhibitor P4 in complex with ASF1 histone chaperone Deposited 2022-12-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–156（156 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290.15 K；0.1 M Tris pH 8.5 30% (w/v) PEG 400	Resolution 2.83 Å R-free 0.221
8BV1 Peptide inhibitor P4 in complex with ASF1 histone chaperone Deposited 2022-12-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–156（156 aa）	Not recorded	GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290.15 K；0.1 M Tris pH 8.5 30% (w/v) PEG 400	Resolution 2.83 Å R-free 0.221
8BV1 Peptide inhibitor P4 in complex with ASF1 histone chaperone Deposited 2022-12-01	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–156（156 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290.15 K；0.1 M Tris pH 8.5 30% (w/v) PEG 400	Resolution 2.83 Å R-free 0.221
8CJ1 Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperone Deposited 2023-02-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–156（156 aa） Chain B 1–156（156 aa） Chain C 1–156（156 aa） Chain D 1–156（156 aa） Chain E 1–156（156 aa） Chain F 1–156（156 aa） Chain G 1–156（156 aa） Chain H 1–156（156 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；290.15 K；0.1 M MES pH 6.5 40% (w/v) PEG 200	Resolution 2.56 Å R-free 0.280
8CJ2 Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone Deposited 2023-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–156（156 aa） Chain B 1–156（156 aa） Chain C 1–156（156 aa） Chain D 1–156（156 aa）	Not recorded	GOL GLYCEROL × 14 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；290.15 K；0.17 M ammonium sulfate 0.085 M NaOAc pH 4.6 25.5% PEG 2000 MME 15% (v/v) glycerol	Resolution 2.13 Å R-free 0.215
8CJ3 Urea-based foldamer inhibitor c3u_7 chimera in complex with ASF1 histone chaperone Deposited 2023-02-11	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–156（156 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290.15 K；0.2 M potassium fluoride 20% (w/v) PEG 3350	Resolution 3.00 Å R-free 0.217
8Z50 Crystal structure of the ASF1-H3T-H4 complex Deposited 2024-04-18	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–173（173 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；1.0 M Lithium chloride, 0.1 M MES pH 6.0, 10% PEG 6000	Resolution 2.80 Å R-free 0.255
9CVC CDAN1 dimer with three ASF1A Deposited 2024-07-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–204（204 aa） Chain D 1–204（204 aa） Chain E 1–204（204 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9IMZ CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate histone supply Deposited 2024-07-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–172（172 aa） Chain D 1–172（172 aa） Chain E 1–172（172 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.75 Å

17 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ASF1A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–157； UniProt 1–155 Author chain B； PDBConstruct 3–157； UniProt 1–155 Author chain C； PDBConstruct 3–157； UniProt 1–155 Author chain D； PDBConstruct 3–157； UniProt 1–155 Author chain E； PDBConstruct 3–157； UniProt 1–155 Author chain F； PDBConstruct 3–157； UniProt 1–155 Author chain G； PDBConstruct 3–157； UniProt 1–155

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	7lny
Deposition date deposition_date	2021-02-08
Structure title title	Apo structure of the Histone chaperone ASF1A residues 1-155
Keywords keywords	;Histone chaperone, immunoglobulin domain-like, protein interaction, replication-coupled nucleosome assembly, replication-independent nucleosome assembly, CELL CYCLE ;; CELL CYCLE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	40.89 Å
Radius of gyration Rg (electron density) rg_electron	40.62 Å
Forward intensity I(0) i0	221351000.00
Molecular weight molecular_weight	122570.0 kDa
Excluded volume excluded_volume	153890 Å³
Envelope volume envelope_volume	219350 Å³
Hydration-shell volume shell_volume	47463 Å³
Envelope diameter envelope_diameter	143.9 Å
Shell Rg shell_rg	42.96 Å
Envelope Rg envelope_rg	40.56 Å
Shape Rg shape_rg	40.61 Å
Total Rg total_rg	40.83 Å
Total atoms total_atoms	16951
Residues n_residues	1078
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	139.0 Å
Rg (real space) rg_real	40.96 Å
Rg uncertainty (real space) rg_real_error	2.02 Å
I(0) (real space) i0_real	2.2140e+08
I(0) uncertainty (real space) i0_real_error	4.3810e+06
Rg (reciprocal space) rg_reciprocal	40.89 Å
I(0) (reciprocal space) i0_reciprocal	221300000.0000
Solution quality estimate total_estimate	0.8775
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	46.3 Å
Skewness Skewness skewness	0.345
Kurtosis Kurtosis kurtosis	-0.346
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	14890000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.803

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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Unit-cell length a length_a	142.282 Å
Unit-cell length b length_b	118.980 Å
Unit-cell length c length_c	109.506 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.45 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	28

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	106.500 Å
R factor r_factor	0.2210
R_work r_work	0.2199
R_free r_free	0.2420

Description description	Histone chaperone ASF1A
Molecular weight formula_weight	17829.9 kDa
Source method src_method	man
Copy count entity_count	7

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G
Atom count atom_count	17416

Apo structure of the Histone chaperone ASF1A residues 1-155

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

Histone chaperone ASF1A

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	465

fit	/app/data/saxs_computation/ln/7lny/7lny.fit
pddf	/app/data/pr_computation/ln/7lny/7lny.pr.out
profile	/app/data/saxs_computation/ln/7lny/7lny.dat