SAXSdb — 2dze

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

Histone chaperone cia1

Schizosaccharomyces pombe

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 3	10-mer peptide from Histone H3.1/H3.2 × 1 （P09988） TRIETHYLENE GLYCOL × 2 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CIA1_SCHPO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–161； UniProt 1–161 Author chain B； PDBConstruct 1–161； UniProt 1–161

10-mer peptide from Histone H3.1/H3.2

OrganismNot specified

UniProt P09988

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 cia1 × 2 （O74515） TRIETHYLENE GLYCOL × 2 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H31_SCHPO
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain X； PDBConstruct 1–10； UniProt 122–131

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	2dze
Deposition date deposition_date	2006-09-28
Structure title title	Crystal structure of histone chaperone Asf1 in complex with a C-terminus of histone H3
Keywords keywords	;Immunoglobulin fold, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, CHAPERONE ;; CHAPERONE
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.

2dze__assembly_1__model_1

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

Download this curve (.dat)

2dze__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2dze__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.77 Å
Rg (electron density)	23.70 Å
Total Rg	24.70 Å
Atom count	2639
Residues	326
Excluded volume	47590 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2dze__assembly_1__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 (4)

Entity 1 Entity 1 polymer

Description description	Histone chaperone cia1
Molecular weight formula_weight	18347.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2858

MSIVNILSVNVLNNPAKFSDPYKFEITFECLEPLKSDLEWKLTYVGSATSQSYDQILDTLLVGPIPIGINKFVFEADPPNIDLLPQLSDVLGVTVILLSCAYEDNEFVRVGYYVNNEMEGLNLQEMDDAEIKKVKVDISKVWRSILAEKPRVTRFNIQWDN

Source Source

Source organism organism	Schizosaccharomyces pombe
Common name common_name	fission yeast
NCBI taxonomy ID ncbi_taxonomy_id	4896
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	10-mer peptide from Histone H3.1/H3.2
Molecular weight formula_weight	1290.6 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X

KDMQLARRLR

Entity 3 Entity 3 non-polymer

Description description	TRIETHYLENE GLYCOL
Molecular weight formula_weight	150.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	219

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2dzea_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.22 — ASF1-like
Family Family family	b.1.22.1 — ASF1-like

Domain ID domain_id	d2dzeb_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.22 — ASF1-like
Family Family family	b.1.22.1 — ASF1-like

CATH v4.4 (2 domains)

Domain ID domain_id	2dzeA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1490 — Histone chaperone ASF1-like

Domain ID domain_id	2dzeB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1490 — Histone chaperone ASF1-like

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Unit-cell length a length_a	40.155 Å
Unit-cell length b length_b	52.130 Å
Unit-cell length c length_c	60.654 Å
Unit-cell angle α angle_alpha	107.35 °
Unit-cell angle β angle_beta	105.94 °
Unit-cell angle γ angle_gamma	93.95 °
Molecules per unit cell Z z_pdb	2

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

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2151
R_work r_work	0.2136
R_free r_free	0.2435

Crystal structure of histone chaperone Asf1 in complex with a C-terminus of histone H3

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

Histone chaperone cia1

State in the Current Structure

Other States of the Same Protein in the Database

10-mer peptide from Histone H3.1/H3.2

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

2dze__assembly_1__model_1

2dze__assembly_1__model_1 | I(q)

2dze__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal structure of histone chaperone Asf1 in complex with a C-terminus of histone H3

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

Histone chaperone cia1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

10-mer peptide from Histone H3.1/H3.2

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

2dze__assembly_1__model_1

2dze__assembly_1__model_1 | I(q)

2dze__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)