1g31

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

Method: X-RAY DIFFRACTION

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

GP31

Enterobacteria phage T4

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 7	PHOSPHATE ION × 19 POTASSIUM ION × 11 water × 7	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 14	PHOSPHATE ION × 38 POTASSIUM ION × 22 water × 14	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VG31_BPT4
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–111； UniProt 1–111 Author chain B； PDBConstruct 1–111； UniProt 1–111 Author chain C； PDBConstruct 1–111； UniProt 1–111 Author chain D； PDBConstruct 1–111； UniProt 1–111 Author chain E； PDBConstruct 1–111； UniProt 1–111 Author chain F； PDBConstruct 1–111； UniProt 1–111 Author chain G； PDBConstruct 1–111； UniProt 1–111

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	1g31
Deposition date deposition_date	1998-03-27
Structure title title	GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4
Keywords keywords	CHAPERONE, CO-CHAPERONIN, GROES, IN VIVO PROTEIN FOLDING, BACTERIOPHAGE T4; CHAPERONE
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.

1g31__assembly_1__model_1

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

Download this curve (.dat)

1g31__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1g31__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	31.26 Å
Rg (electron density)	30.53 Å
Total Rg	31.27 Å
Atom count	5798
Residues	749
Excluded volume	104370 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1g31__assembly_1__model_1`	heptameric （7）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1g31__assembly_2__model_1`	tetradecameric （14）	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	GP31
Molecular weight formula_weight	12092.0 kDa
Source method src_method	man
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G
Atom count atom_count	6267

MSEVQQLPIRAVGEYVILVSEPAQAGDEEVTESGLIIGKRVQGEVPELCVVHSVGPDVPEGFCEVGDLTSLPVGQIRNVPHPFVALGLKQPKEIKQKFVTCHYKAIPCLYK

Source Source

Source organism organism	Enterobacteria phage T4
NCBI taxonomy ID ncbi_taxonomy_id	10665
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	19

Entity 3 Entity 3 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	11

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	469

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6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

Domain ID domain_id	d1g31a_
Class class	b — All beta proteins
Fold Fold fold	b.35 — GroES-like
Superfamily Superfamily superfamily	b.35.1 — GroES-like
Family Family family	b.35.1.1 — GroES

Domain ID domain_id	d1g31b_
Class class	b — All beta proteins
Fold Fold fold	b.35 — GroES-like
Superfamily Superfamily superfamily	b.35.1 — GroES-like
Family Family family	b.35.1.1 — GroES

Domain ID domain_id	d1g31c_
Class class	b — All beta proteins
Fold Fold fold	b.35 — GroES-like
Superfamily Superfamily superfamily	b.35.1 — GroES-like
Family Family family	b.35.1.1 — GroES

Domain ID domain_id	d1g31d_
Class class	b — All beta proteins
Fold Fold fold	b.35 — GroES-like
Superfamily Superfamily superfamily	b.35.1 — GroES-like
Family Family family	b.35.1.1 — GroES

Domain ID domain_id	d1g31e_
Class class	b — All beta proteins
Fold Fold fold	b.35 — GroES-like
Superfamily Superfamily superfamily	b.35.1 — GroES-like
Family Family family	b.35.1.1 — GroES

Domain ID domain_id	d1g31f_
Class class	b — All beta proteins
Fold Fold fold	b.35 — GroES-like
Superfamily Superfamily superfamily	b.35.1 — GroES-like
Family Family family	b.35.1.1 — GroES

Domain ID domain_id	d1g31g_
Class class	b — All beta proteins
Fold Fold fold	b.35 — GroES-like
Superfamily Superfamily superfamily	b.35.1 — GroES-like
Family Family family	b.35.1.1 — GroES

CATH v4.4 (7 domains)

Domain ID domain_id	1g31A00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	33 — 10 Kd Chaperonin, Protein Cpn10; Chain O
Homologous superfamily homologous superfamily	40 — GroES chaperonin

Domain ID domain_id	1g31B00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	33 — 10 Kd Chaperonin, Protein Cpn10; Chain O
Homologous superfamily homologous superfamily	40 — GroES chaperonin

Domain ID domain_id	1g31C00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	33 — 10 Kd Chaperonin, Protein Cpn10; Chain O
Homologous superfamily homologous superfamily	40 — GroES chaperonin

Domain ID domain_id	1g31D00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	33 — 10 Kd Chaperonin, Protein Cpn10; Chain O
Homologous superfamily homologous superfamily	40 — GroES chaperonin

Domain ID domain_id	1g31E00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	33 — 10 Kd Chaperonin, Protein Cpn10; Chain O
Homologous superfamily homologous superfamily	40 — GroES chaperonin

Domain ID domain_id	1g31F00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	33 — 10 Kd Chaperonin, Protein Cpn10; Chain O
Homologous superfamily homologous superfamily	40 — GroES chaperonin

Domain ID domain_id	1g31G00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	33 — 10 Kd Chaperonin, Protein Cpn10; Chain O
Homologous superfamily homologous superfamily	40 — GroES chaperonin

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Unit-cell length a length_a	157.677 Å
Unit-cell length b length_b	157.677 Å
Unit-cell length c length_c	90.932 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	56

Space group space_group	P 42 21 2
Space-group number int_tables_number	94
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2250
R_work r_work	0.2250
R_free r_free	0.2540

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

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

GP31

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

1g31__assembly_1__model_1

1g31__assembly_1__model_1 | I(q)

1g31__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

CATH v4.4 (7 domains)

7. Citations (4)

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4

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

GP31

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

1g31__assembly_1__model_1

1g31__assembly_1__model_1 | I(q)

1g31__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

CATH v4.4 (7 domains)

7. Citations (4)