SAXSdb — 1ei3

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

FIBRINOGEN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	FIBRINOGEN × 2 （Q02020） FIBRINOGEN × 2 （O93568）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FIBA_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–491； UniProt 19–509 Author chain D； PDBConstruct 1–491； UniProt 19–509

FIBRINOGEN

OrganismNot specified

UniProt Q02020

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	FIBRINOGEN × 2 （P14448） FIBRINOGEN × 2 （O93568）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FIBB_CHICK
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–464； UniProt 1–463 Author chain E； PDBConstruct 2–464； UniProt 1–463

FIBRINOGEN

OrganismNot specified

UniProt O93568

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	FIBRINOGEN × 2 （P14448） FIBRINOGEN × 2 （Q02020）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O93568_CHICK
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–409； UniProt 27–435 Author chain F； PDBConstruct 1–409； UniProt 27–435

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	1ei3
Deposition date deposition_date	2000-02-23
Structure title title	CRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGEN
Keywords keywords	coiled coils, disulfide rings, fibrin forming entities, 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.

1ei3__assembly_1__model_1

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

Download this curve (.dat)

1ei3__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1ei3__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	0.00 Å
Rg (electron density)	155.70 Å
Total Rg	154.80 Å
Atom count	0
Residues	0
Excluded volume	262330 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1ei3__assembly_1__model_1`	hexameric （6）	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	FIBRINOGEN
Molecular weight formula_weight	54288.0 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	1896

QDGKTTFEKEGGGGRGPRILENMHESSCKYEKNWPICVDDDWGTKCPSCCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKGTQK

Entity 2 Entity 2 polymer

Description description	FIBRINOGEN
Molecular weight formula_weight	52874.3 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

QASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPIIYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKFSDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNLDNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVSGRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQDGSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPTKVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGASQLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYFPD

Entity 3 Entity 3 polymer

Description description	FIBRINOGEN
Molecular weight formula_weight	47000.1 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,F

YIATRENCCILDERFGSYCPTTCGIADFFNKYRLTTDGELLEIEGLLQQATNSTGSIEYLIQHIKTIYPSEKQTLPQSIEQLTQKSKKIIEEIIRYENTILAHENTIQQLTDMHIMNSNKITQLKQKIAQLESHCQEPCKDTAEIQETTGRDCQDIANKGARKSGLYFIKPQKAKQSFLVYCEIDTYGNGWTVLQRRLDGSEDFRRNWVQYKEGFGHLSPDDTTEFWLGNEKIHLITTQSTLPYALRIELEDWSGKKGTADYAVFKVGTEEDKYRLTYAYFIGGERGDAFDGFNFGDDPSDKSYTYHNGMRFSTFDNDNDNFEGNCAEQDGSGWWMNRCHAGHLNGPYYIGGVYSRDTGTNSYDNGIIWATWRDRWYSMKKTTMKIIPFNRLSIDGQQHSGGLKQVGDS

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1ei3a_
Class class	i — Low resolution protein structures
Fold Fold fold	i.9 — Blood clotting
Superfamily Superfamily superfamily	i.9.1 — Blood clotting
Family Family family	i.9.1.1 — Blood clotting

Domain ID domain_id	d1ei3b_
Class class	i — Low resolution protein structures
Fold Fold fold	i.9 — Blood clotting
Superfamily Superfamily superfamily	i.9.1 — Blood clotting
Family Family family	i.9.1.1 — Blood clotting

Domain ID domain_id	d1ei3c_
Class class	i — Low resolution protein structures
Fold Fold fold	i.9 — Blood clotting
Superfamily Superfamily superfamily	i.9.1 — Blood clotting
Family Family family	i.9.1.1 — Blood clotting

Domain ID domain_id	d1ei3d_
Class class	i — Low resolution protein structures
Fold Fold fold	i.9 — Blood clotting
Superfamily Superfamily superfamily	i.9.1 — Blood clotting
Family Family family	i.9.1.1 — Blood clotting

Domain ID domain_id	d1ei3e_
Class class	i — Low resolution protein structures
Fold Fold fold	i.9 — Blood clotting
Superfamily Superfamily superfamily	i.9.1 — Blood clotting
Family Family family	i.9.1.1 — Blood clotting

Domain ID domain_id	d1ei3f_
Class class	i — Low resolution protein structures
Fold Fold fold	i.9 — Blood clotting
Superfamily Superfamily superfamily	i.9.1 — Blood clotting
Family Family family	i.9.1.1 — Blood clotting

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Unit-cell length a length_a	114.726 Å
Unit-cell length b length_b	101.849 Å
Unit-cell length c length_c	210.232 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	106.71 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	5.500 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

CRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGEN

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

FIBRINOGEN

State in the Current Structure

Other States of the Same Protein in the Database

FIBRINOGEN

State in the Current Structure

Other States of the Same Protein in the Database

FIBRINOGEN

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

1ei3__assembly_1__model_1

1ei3__assembly_1__model_1 | I(q)

1ei3__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

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

7. Citations (3)

CRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGEN

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

FIBRINOGEN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

FIBRINOGEN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

FIBRINOGEN

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

1ei3__assembly_1__model_1

1ei3__assembly_1__model_1 | I(q)

1ei3__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

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

7. Citations (3)