SAXSdb — 7lo0

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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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Serine/threonine-protein kinase tousled-like 2 × 2 （Q86UE8） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Serine/threonine-protein kinase tousled-like 2 × 2 （Q86UE8） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Serine/threonine-protein kinase tousled-like 2 × 2 （Q86UE8） water × 3	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	Serine/threonine-protein kinase tousled-like 2 × 2 （Q86UE8） water × 3	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 3	Serine/threonine-protein kinase tousled-like 2 × 2 （Q86UE8） water × 2	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 3	Serine/threonine-protein kinase tousled-like 2 × 2 （Q86UE8） water × 2	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 3	Serine/threonine-protein kinase tousled-like 2 × 2 （Q86UE8） water × 1	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 3	Serine/threonine-protein kinase tousled-like 2 × 2 （Q86UE8） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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 Author chain H； PDBConstruct 3–157； UniProt 1–155

Serine/threonine-protein kinase tousled-like 2

Homo sapiens

UniProt Q86UE8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	Histone chaperone ASF1A × 1 （Q9Y294） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	Histone chaperone ASF1A × 1 （Q9Y294） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 3	Histone chaperone ASF1A × 1 （Q9Y294） water × 3	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 3	Histone chaperone ASF1A × 1 （Q9Y294） water × 3	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 3	Histone chaperone ASF1A × 1 （Q9Y294） water × 2	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 3	Histone chaperone ASF1A × 1 （Q9Y294） water × 2	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 3	Histone chaperone ASF1A × 1 （Q9Y294） water × 1	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 3	Histone chaperone ASF1A × 1 （Q9Y294） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TLK2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain I； PDBConstruct 1–21； UniProt 3–23 Author chain J； PDBConstruct 1–21； UniProt 3–23 Author chain K； PDBConstruct 1–21； UniProt 3–23 Author chain L； PDBConstruct 1–21； UniProt 3–23 Author chain M； PDBConstruct 1–21； UniProt 3–23 Author chain N； PDBConstruct 1–21； UniProt 3–23 Author chain O； PDBConstruct 1–21； UniProt 3–23 Author chain P； PDBConstruct 1–21； UniProt 3–23 Author chain Q； PDBConstruct 1–21； UniProt 3–23 Author chain R； PDBConstruct 1–21； UniProt 3–23 Author chain T； PDBConstruct 1–21； UniProt 3–23 Author chain U； PDBConstruct 1–21； UniProt 3–23 Author chain V； PDBConstruct 1–21； UniProt 3–23 Author chain W； PDBConstruct 1–21； UniProt 3–23 Author chain X； PDBConstruct 1–21； UniProt 3–23 Author chain Y； PDBConstruct 1–21； UniProt 3–23

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	7lo0
Deposition date deposition_date	2021-02-08
Structure title title	Structure of human ASF1a in complex with a TLK2 peptide
Keywords keywords	histone chaperone, kinase, docking, nucleosome assembly, CELL CYCLE; CELL CYCLE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

7lo0__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

7lo0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

7lo0__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	18.47 Å
Rg (electron density)	17.34 Å
Total Rg	18.35 Å
Atom count	2812
Residues	176
Excluded volume	25337 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`7lo0__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`7lo0__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`7lo0__assembly_3__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`7lo0__assembly_4__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`7lo0__assembly_5__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`7lo0__assembly_6__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`7lo0__assembly_7__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`7lo0__assembly_8__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Histone chaperone ASF1A
Molecular weight formula_weight	17829.9 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	22462

GSMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWED

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Serine/threonine-protein kinase tousled-like 2
Molecular weight formula_weight	2499.8 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	man
Copy count entity_count	16

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,J,K,L,M,N,O,P,Q,R,T,U,V,W,X,Y

EELHSLDPRRQELLEARFTGV

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	166

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Unit-cell length a length_a	88.023 Å
Unit-cell length b length_b	136.681 Å
Unit-cell length c length_c	101.316 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.22 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	32

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.710 Å
Low-resolution limit resolution_low	98.630 Å
R factor r_factor	0.2137
R_work r_work	0.2130
R_free r_free	0.2256

Structure of human ASF1a in complex with a TLK2 peptide

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

Serine/threonine-protein kinase tousled-like 2

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

7lo0__assembly_1__model_1

7lo0__assembly_1__model_1 | I(q)

7lo0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

7. Citations (1)

Structure of human ASF1a in complex with a TLK2 peptide

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

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Serine/threonine-protein kinase tousled-like 2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

7lo0__assembly_1__model_1

7lo0__assembly_1__model_1 | I(q)

7lo0__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

7. Citations (1)