SAXSdb — 6qpq

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

Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein

Chaetomium thermophilum var. thermophilum DSM 1495

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Sister chromatid cohesion protein 1 × 1 （Q12158） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Sister chromatid cohesion protein 1 × 1 （Q12158） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	G0SGH3_CHATD
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–242； UniProt 1–242 Author chain A； PDBConstruct 251–451； UniProt 1064–1264 Author chain C； PDBConstruct 1–242； UniProt 1–242 Author chain C； PDBConstruct 251–451； UniProt 1064–1264

Sister chromatid cohesion protein 1

Saccharomyces cerevisiae S288C

UniProt Q12158

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein × 1 （G0SGH3） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein × 1 （G0SGH3） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SCC1_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–566； UniProt 1–566 Author chain D； PDBConstruct 1–566； UniProt 1–566

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	6qpq
Deposition date deposition_date	2019-02-14
Structure title title	The structure of the cohesin head module elucidates the mechanism of ring opening
Keywords keywords	Cohesin, cell division, genome regulation, sister chromatid cohesion, SMC, kleisin, 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.

6qpq__assembly_1__model_1

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

Download this curve (.dat)

6qpq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6qpq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	32.73 Å
Rg (electron density)	33.40 Å
Total Rg	33.57 Å
Atom count	7804
Residues	483
Excluded volume	69466 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6qpq__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6qpq__assembly_2__model_1`	dimeric （2）	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	Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein
Molecular weight formula_weight	51883.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	15820

MGKLIRLELFNFKSYKGHHTLLFGDSYFTSIIGPNGSGKSNSMDAISFVLGIKSSHLRSSNLRDLIYRGRVMKTSKIQDDGTTAPATNGDVNGYENGDAGDDEDTSQRTSRNDPKTAWVMAVYEDDAGELHRWKRTITANGTSEYRINDRVVNAQQYNEALEKENILIKARNFLVFQGDVEAIASQSPQDLTRLIEQISGSLEYKEEYERLEEEVRQATEEQAYKLQRRRAANSEIKQYMEQSPGLEVLFMDRLDHVRKQLEQTEQEFEASKAKLRQARESFQAVKQKRLELFNKAFTHIQEQITHVYKELTRSEAYPLGGQAYLDIEEDTDTPFLSGVKYHAMPPLKRFRDMEHLSGGEKTMAALALLFAIHSYQPSPFFVLDEVDAALDNANVEKIKKYIREHAGPGMQFIVISLKPALFQASESLIGVYRDQEANTSRTLTLDLRKYRHH

Source Source

Source organism organism	Chaetomium thermophilum var. thermophilum DSM 1495
NCBI taxonomy ID ncbi_taxonomy_id	759272
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Sister chromatid cohesion protein 1
Molecular weight formula_weight	63352.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

MVTENPQRLTVLRLATNKGPLAQIWLASNMSNIPRGSVIQTHIAESAKEIAKASGCDDESGDNEYITLRTSGELLQGIVRVYSKQATFLLTDIKDTLTKISMLFKTSQKMTSTVNRLNTVTRVHQLMLEDAVTEREVLVTPGLEFLDDTTIPVGLMAQENSMERKVQGAAPWDTSLEVGRRFSPDEDFEHNNLSSMNLDFDIEEGPITSKSWEEGTRQSSRNFDTHENYIQDDDFPLDDAGTIGWDLGITEKNDQNNDDDDNSVEQGRRLGESIMSEEPTDFGFDLDIEKEAPAGNIDTITDAMTESQPKQTGTRRNSKLLNTKSIQIDEETENSESIASSNTYKEERSNNLLTPQPTNFTTKRLWSEITESMSYLPDPILKNFLSYESLKKRKIHNGREGSIEEPELNVSLNLTDDVISNAGTNDNSFNELTDNMSDFVPIDAGLNEAPFPEENIIDAKTRNEQTTIQTEKVRPTPGEVASKAIVQMAKILRKELSEEKEVIFTDVLKSQANTEPENITKREASRGFFDILSLATEGCIGLSQTEAFGNIKIDAKPALFERFINA

Source Source

Source organism organism	Saccharomyces cerevisiae S288C
NCBI taxonomy ID ncbi_taxonomy_id	559292
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	343

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d6qpqa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.0 — automated matches

Domain ID domain_id	d6qpqa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d6qpqb_
Class class	a — All alpha proteins
Fold Fold fold	a.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamily	a.4.5 — 'Winged helix' DNA-binding domain
Family Family family	a.4.5.0 — automated matches

Domain ID domain_id	d6qpqc1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.0 — automated matches

Domain ID domain_id	d6qpqc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d6qpqd_
Class class	a — All alpha proteins
Fold Fold fold	a.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamily	a.4.5 — 'Winged helix' DNA-binding domain
Family Family family	a.4.5.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	6qpqB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	580 — Structural maintenance of chromosome 1. Chain E

Domain ID domain_id	6qpqD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	580 — Structural maintenance of chromosome 1. Chain E

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Unit-cell length a length_a	80.752 Å
Unit-cell length b length_b	111.130 Å
Unit-cell length c length_c	166.195 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	8

Space group space_group	P 2 21 21
Space-group number int_tables_number	18
Crystal system crystal_system	orthorhombic

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	45.700 Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

The structure of the cohesin head module elucidates the mechanism of ring opening

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

Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein

State in the Current Structure

Other States of the Same Protein in the Database

Sister chromatid cohesion protein 1

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

6qpq__assembly_1__model_1

6qpq__assembly_1__model_1 | I(q)

6qpq__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

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (6 domains)

CATH v4.4 (2 domains)

7. Citations (1)

The structure of the cohesin head module elucidates the mechanism of ring opening

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

Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Sister chromatid cohesion protein 1

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

6qpq__assembly_1__model_1

6qpq__assembly_1__model_1 | I(q)

6qpq__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

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (6 domains)

CATH v4.4 (2 domains)

7. Citations (1)