SAXSdb — 1gff

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

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

Enterobacteria phage G4

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 60 （P03644） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 60 （P03652）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03644） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03652）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 15	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 5 （P03644） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 5 （P03652）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 18	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 6 （P03644） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 6 （P03652）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 3	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03644） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03652）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 60	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 20 （P03644） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 20 （P03652）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VGF_BPG4
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–426； UniProt 1–426

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

Enterobacteria phage G4

UniProt P03644

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 60 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 60 （P03652）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03652）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 15	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 5 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 5 （P03652）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 18	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 6 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 6 （P03652）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 3	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03652）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 60	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 20 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 20 （P03652）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VGG_BPG4
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain 2； PDBConstruct 1–177； UniProt 1–177

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

OrganismNot specified

UniProt P03652

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 180	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 60 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 60 （P03644）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 3	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03644）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 15	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 5 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 5 （P03644）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 18	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 6 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 6 （P03644）	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 3	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 1 （P03644）	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 60	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 20 （P03642） BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ × 20 （P03644）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VGJ_BPG4
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain 3； PDBConstruct 1–25； UniProt 1–25

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	1gff
Deposition date deposition_date	1995-11-06
Structure title title	THE ATOMIC STRUCTURE OF THE DEGRADED PROCAPSID PARTICLE OF THE BACTERIOPHAGE G4: INDUCED STRUCTURAL CHANGES IN THE PRESENCE OF CALCIUM IONS AND FUNCTIONAL IMPLICATIONS
Keywords keywords	COAT PROTEIN, Icosahedral virus, Virus; VIRUS
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.

1gff__assembly_1__model_1

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

Download this curve (.dat)

1gff__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gff__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)	126.70 Å
Total Rg	127.00 Å
Atom count	286740
Residues	36360
Excluded volume	5086200 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gff__assembly_1__model_1`	complete icosahedral assembly （180）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1gff__assembly_2__model_1`	trimeric （3）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3	1	`1gff__assembly_3__model_1`	pentadecameric （15）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
4	1	`1gff__assembly_4__model_1`	octadecameric （18）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
5	1	`1gff__assembly_5__model_1`	trimeric （3）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
6	1	`1gff__assembly_6__model_1`	60-meric （60）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.

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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	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ
Molecular weight formula_weight	48611.6 kDa
Mutation mutation	AM(E)W4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1
Atom count atom_count	4779

SNVQTSADRVPHDLSHLVFEAGKIGRLKTISWTPVVAGDSFECDMVGAIRLSPLRRGLAVDSRVDIFSFYIPHRHIYGQQWINFMKDGVNASPLPPVTCSSGWDSAAYLGTIPSSTLKVPKFLHQGYLNIYNNYFKPPWSDDLTYANPSNMPSEDYKWGVRVANLKSIWTAPLPPDTRTSENMTTGTSTIDIMGLQAAYAKLHTEQERDYFMTRYRDIMKEFGGHTSYDGDNRPLLLMRSEFWASGYDVDGTDQSSLGQFSGRVQQTFNHKVPRFYVPEHGVIMTLAVTRFPPTHEMEMHYLVGKENLTYTDIACDPALMANLPPREVSLKEFFHSSPDSAKFKIAEGQWYRTQPDRVAFPYNALDGFPFYSALPSTDLKDRVLVNTNNYDEIFQSMQLAHWNMQTKFNINVYRHMPTTRDSIMTS

Source Source

Source organism organism	Enterobacteria phage G4
NCBI taxonomy ID ncbi_taxonomy_id	10843
Host organism host_organism	Escherichia coli C

Entity 2 Entity 2 polymer

Description description	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ
Molecular weight formula_weight	18837.4 kDa
Mutation mutation	AM(E)W4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

MFQKFISKHNAPINSTQLAATKTPAVAAPVLSVPNLSRSTILINATTTAVTTHSGLCHVVRIDETNPTNHHALSIAGSLSNVPADMIAFAIRFEVADGVVPTAVPALYDVYPIETFNNGKAISFKDAVTIDSHPRTVGNDVYAGIMLWSNAWTASTISGVLSVNQVNREATVLQPLK

Source Source

Source organism organism	Enterobacteria phage G4
NCBI taxonomy ID ncbi_taxonomy_id	10843
Host organism host_organism	Escherichia coli C

Entity 3 Entity 3 polymer

Description description	BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ
Molecular weight formula_weight	2822.3 kDa
Mutation mutation	AM(E)W4
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3

MKKSIRRSGGKSKGARLWYVGGTQY

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1gff1_
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.5 — ssDNA viruses
Family Family family	b.121.5.1 — Microviridae-like VP

Domain ID domain_id	d1gff2_
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.5 — ssDNA viruses
Family Family family	b.121.5.1 — Microviridae-like VP

CATH v4.4 (2 domains)

Domain ID domain_id	1gff100
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	169 — Bacteriophage G4 Capsid Proteins Gpf, Gpg, Gpj, subunit 1
Homologous superfamily homologous superfamily	10 — Microviridae F protein

Domain ID domain_id	1gff200
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

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Unit-cell length a length_a	414.200 Å
Unit-cell length b length_b	414.200 Å
Unit-cell length c length_c	263.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	120

Space group space_group	P 63 2 2
Space-group number int_tables_number	182
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	—
R_work r_work	0.3520
R_free r_free	—

THE ATOMIC STRUCTURE OF THE DEGRADED PROCAPSID PARTICLE OF THE BACTERIOPHAGE G4: INDUCED STRUCTURAL CHANGES IN THE PRESENCE OF CALCIUM IONS AND FUNCTIONAL IMPLICATIONS

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

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

State in the Current Structure

Other States of the Same Protein in the Database

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

State in the Current Structure

Other States of the Same Protein in the Database

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

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

1gff__assembly_1__model_1

1gff__assembly_1__model_1 | I(q)

1gff__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (5)

THE ATOMIC STRUCTURE OF THE DEGRADED PROCAPSID PARTICLE OF THE BACTERIOPHAGE G4: INDUCED STRUCTURAL CHANGES IN THE PRESENCE OF CALCIUM IONS AND FUNCTIONAL IMPLICATIONS

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

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

BACTERIOPHAGE G4 CAPSID PROTEINS GPF, GPG, GPJ

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

1gff__assembly_1__model_1

1gff__assembly_1__model_1 | I(q)

1gff__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (5)