1deq

THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)

Method: X-RAY DIFFRACTION

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

FIBRINOGEN (ALPHA CHAIN)

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 7	FIBRINOGEN (BETA CHAIN) × 2 （P02676） FIBRINOGEN (GAMMA CHAIN) × 2 （P12799） FIBRINOGEN × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 7	FIBRINOGEN (BETA CHAIN) × 2 （P02676） FIBRINOGEN (GAMMA CHAIN) × 2 （P12799） FIBRINOGEN × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FIBA_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–390； UniProt 20–409 Author chain D； PDBConstruct 1–390； UniProt 20–409 Author chain N； PDBConstruct 1–390； UniProt 20–409 Author chain Q； PDBConstruct 1–390； UniProt 20–409

FIBRINOGEN (BETA CHAIN)

OrganismNot specified

UniProt P02676

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 7	FIBRINOGEN (ALPHA CHAIN) × 2 （P02672） FIBRINOGEN (GAMMA CHAIN) × 2 （P12799） FIBRINOGEN × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 7	FIBRINOGEN (ALPHA CHAIN) × 2 （P02672） FIBRINOGEN (GAMMA CHAIN) × 2 （P12799） FIBRINOGEN × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FIBB_BOVIN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–408； UniProt 61–468 Author chain E； PDBConstruct 1–408； UniProt 61–468 Author chain O； PDBConstruct 1–408； UniProt 61–468 Author chain R； PDBConstruct 1–408； UniProt 61–468

FIBRINOGEN (GAMMA CHAIN)

OrganismNot specified

UniProt P12799

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 7	FIBRINOGEN (ALPHA CHAIN) × 2 （P02672） FIBRINOGEN (BETA CHAIN) × 2 （P02676） FIBRINOGEN × 1	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 7	FIBRINOGEN (ALPHA CHAIN) × 2 （P02672） FIBRINOGEN (BETA CHAIN) × 2 （P02676） FIBRINOGEN × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FIBG_BOVIN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–407； UniProt 25–432 Author chain F； PDBConstruct 1–407； UniProt 25–432 Author chain P； PDBConstruct 1–407； UniProt 25–432 Author chain S； PDBConstruct 1–407； UniProt 25–432

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	1deq
Deposition date deposition_date	1999-11-15
Structure title title	THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)
Keywords keywords	COILED-COIL, 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.

1deq__assembly_1__model_1

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

Download this curve (.dat)

1deq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1deq__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)	152.10 Å
Total Rg	151.20 Å
Atom count	0
Residues	0
Excluded volume	278440 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1deq__assembly_1__model_1`	heptameric （7）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1deq__assembly_2__model_1`	heptameric （7）	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	FIBRINOGEN (ALPHA CHAIN)
Molecular weight formula_weight	42767.4 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D,N,Q
Atom count atom_count	3900

EDGSDPPSGDFLTEGGGVRGPRLVERQQSACKETGWPFCSDEDWNTKCPSGCRMKGLIDEVDQDFTSRINKLRDSLFNYQKNSKDSNTLTKNIVELMRGDFAKANNNDNTFKQINEDLRSRIEILRRKVIEQVQRINLLQKNVRDQLVDMKRLEVDIDIKIRSCKGSCSRALEHKVDLEDYKNQQKQLEQVIAINLLPSRDIQYLPILKMSTITGPVPREFKSQLQEAPLEWKALLEMQQTKMVLETFGGDGHARGDSVSQGTGLAPGSPRKPGTSSIGNVNPGSYGPGSSGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNTGSSGSSSFRPDSSGHGNIRPSSPDWGTFR

Entity 2 Entity 2 polymer

Description description	FIBRINOGEN (BETA CHAIN)
Molecular weight formula_weight	46901.6 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

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

KVERKPPDADGCLHADPDLGVLCPTGCKLQDTLVRQERPIRKSIEDLRNTVDSVSRTSSSTFQYITLLKNMWKGRQNQVQDNENVVNEYSSHLEKHQLYIDETVKNNIPTKLRVLRSILENLRSKIQKLESDVSTQMEYCRTPCTVTCNIPVVSGKECEKIIRNEGETSEMYLIQPEDSSKPYRVYCDMKTEKGGWTVIQNRQDGSVDFGRKWDPYKQGFGNIATNAEGKKYCGVPGEYWLGNDRISQLTNMGPTKLLIEMEDWKGDKVTALYEGFTVQNEANKYQLSVSKYKGTAGNALIEGASQLVGENRTMTIHNSMFFSTYDRDNDGWKTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGAYTWDMAKHGTDDGVVWMNWQGSWYSMKKMSKMIRPYFPEQ

Entity 3 Entity 3 polymer

Description description	FIBRINOGEN (GAMMA CHAIN)
Molecular weight formula_weight	46626.6 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

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

YVATRDNCCILDERFGSYCPTTCGIADFLNNYQTSVDKDLRTLEGILYQVENKTSEARELVKAIQISYNPDQPSKPNNIESATKNSKSMMEEIMKYETLISTHESTIRFLQEIYNSNSQKIVNLRDKVVQLEANCQEPCQDTVKIHDVTGRDCQDVANKGAKESGLYFIRPLKAKQQFLVYCEIDGSGNGWTVFQKRLDGSLDFKKNWIQYKEGFGHLSPTGNTEFWLGNEKIHLISTQSTIPYVLRIQLEDWNGRTSTADYASFKVTGENDKYRLTYAYFIGGDAGDAFDGYDFGDDSSDKFFTSHNGMQFSTWDSDNDKYDGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKTSTPNGYDNGIIWATWKSRWYSMKKTTMKIIPLNRLAIGEGQQHQLGGAKQAGDV

Entity 4 Entity 4 polymer

Description description	FIBRINOGEN
Molecular weight formula_weight	7677.5 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M,Z

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

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6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (14 domains)

Domain ID domain_id	d1deqa_
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	d1deqb_
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	d1deqc_
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	d1deqd_
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	d1deqe_
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	d1deqf_
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	d1deqm_
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	d1deqn_
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	d1deqo_
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	d1deqp_
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	d1deqq_
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	d1deqr_
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	d1deqs_
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	d1deqz_
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	176.006 Å
Unit-cell length b length_b	94.935 Å
Unit-cell length c length_c	209.805 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	94.41 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	3.500 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.2630
R_work r_work	0.2570
R_free r_free	0.3700

THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)

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

FIBRINOGEN (ALPHA CHAIN)

State in the Current Structure

Other States of the Same Protein in the Database

FIBRINOGEN (BETA CHAIN)

State in the Current Structure

Other States of the Same Protein in the Database

FIBRINOGEN (GAMMA CHAIN)

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

1deq__assembly_1__model_1

1deq__assembly_1__model_1 | I(q)

1deq__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (14 domains)

7. Citations (4)

THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)

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

FIBRINOGEN (ALPHA CHAIN)

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 (BETA CHAIN)

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 (GAMMA CHAIN)

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

1deq__assembly_1__model_1

1deq__assembly_1__model_1 | I(q)

1deq__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (14 domains)

7. Citations (4)