SAXSdb — 6szw

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

Complement component 1 Q subcomponent-binding protein, mitochondrial

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Coagulation factor XII × 1 （P00748） ZINC ION × 3 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	C1QBP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–209； UniProt 75–282 Author chain B； PDBConstruct 2–209； UniProt 75–282 Author chain C； PDBConstruct 2–209； UniProt 75–282

Coagulation factor XII

Homo sapiens

UniProt P00748

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Complement component 1 Q subcomponent-binding protein, mitochondrial × 3 （Q07021） ZINC ION × 3 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FA12_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–71； UniProt 20–90

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	6szw
Deposition date deposition_date	2019-10-02
Structure title title	Asymmetric complex of Factor XII and kininogen with gC1qR/C1QBP/P32 is governed by allostery
Keywords keywords	Contact activation, BLOOD CLOTTING; BLOOD CLOTTING
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.

6szw__assembly_1__model_1

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

Download this curve (.dat)

6szw__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6szw__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.55 Å
Rg (electron density)	28.79 Å
Total Rg	29.59 Å
Atom count	4728
Residues	588
Excluded volume	83547 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6szw__assembly_1__model_1`	tetrameric （4）	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	Complement component 1 Q subcomponent-binding protein, mitochondrial
Molecular weight formula_weight	23826.1 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	4739

MHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ

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	Coagulation factor XII
Molecular weight formula_weight	8461.5 kDa
EC 编号 ec_number	3.4.21.38
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

IPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLE

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Drosophila melanogaster

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	11

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

Domain ID domain_id	d6szwa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.25 — Mitochondrial glycoprotein MAM33-like
Superfamily Superfamily superfamily	d.25.1 — Mitochondrial glycoprotein MAM33-like
Family Family family	d.25.1.1 — Mitochondrial glycoprotein MAM33-like

Domain ID domain_id	d6szwa2
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	d6szwb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.25 — Mitochondrial glycoprotein MAM33-like
Superfamily Superfamily superfamily	d.25.1 — Mitochondrial glycoprotein MAM33-like
Family Family family	d.25.1.1 — Mitochondrial glycoprotein MAM33-like

Domain ID domain_id	d6szwb2
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	d6szwc1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.25 — Mitochondrial glycoprotein MAM33-like
Superfamily Superfamily superfamily	d.25.1 — Mitochondrial glycoprotein MAM33-like
Family Family family	d.25.1.1 — Mitochondrial glycoprotein MAM33-like

Domain ID domain_id	d6szwc2
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	d6szwd_
Class class	g — Small proteins
Fold Fold fold	g.14 — Kringle-like
Superfamily Superfamily superfamily	g.14.1 — Kringle-like
Family Family family	g.14.1.0 — automated matches

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Unit-cell length a length_a	106.290 Å
Unit-cell length b length_b	71.560 Å
Unit-cell length c length_c	115.857 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	110.64 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

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

Resolution resolution	3.140 Å
Low-resolution limit resolution_low	90.990 Å
R factor r_factor	0.1981
R_work r_work	0.1952
R_free r_free	0.2505

Asymmetric complex of Factor XII and kininogen with gC1qR/C1QBP/P32 is governed by allostery

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

Complement component 1 Q subcomponent-binding protein, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Coagulation factor XII

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

6szw__assembly_1__model_1

6szw__assembly_1__model_1 | I(q)

6szw__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

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

7. Citations (1)

Asymmetric complex of Factor XII and kininogen with gC1qR/C1QBP/P32 is governed by allostery

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

Complement component 1 Q subcomponent-binding protein, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Coagulation factor XII

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

6szw__assembly_1__model_1

6szw__assembly_1__model_1 | I(q)

6szw__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

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

7. Citations (1)