SAXSdb — 2cgt

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

60 KDA GROEL

ESCHERICHIA COLI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 21	CAPSID ASSEMBLY PROTEIN GP31 × 7 （P17313）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CH60_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–547； UniProt 1–547 Author chain B； PDBConstruct 1–547； UniProt 1–547 Author chain C； PDBConstruct 1–547； UniProt 1–547 Author chain D； PDBConstruct 1–547； UniProt 1–547 Author chain E； PDBConstruct 1–547； UniProt 1–547 Author chain F； PDBConstruct 1–547； UniProt 1–547 Author chain G； PDBConstruct 1–547； UniProt 1–547 Author chain H； PDBConstruct 1–547； UniProt 1–547 Author chain I； PDBConstruct 1–547； UniProt 1–547 Author chain J； PDBConstruct 1–547； UniProt 1–547 Author chain K； PDBConstruct 1–547； UniProt 1–547 Author chain L； PDBConstruct 1–547； UniProt 1–547 Author chain M； PDBConstruct 1–547； UniProt 1–547 Author chain N； PDBConstruct 1–547； UniProt 1–547

CAPSID ASSEMBLY PROTEIN GP31

BACTERIOPHAGE T4

UniProt P17313

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 21	60 KDA GROEL × 14 （P0A6F5）	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	2
Chains and sequence ranges	Author chain O； PDBConstruct 1–111； UniProt 1–111 Author chain P； PDBConstruct 1–111； UniProt 1–111 Author chain Q； PDBConstruct 1–111； UniProt 1–111 Author chain R； PDBConstruct 1–111； UniProt 1–111 Author chain S； PDBConstruct 1–111； UniProt 1–111 Author chain T； PDBConstruct 1–111； UniProt 1–111 Author chain U； 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	2cgt
Deposition date deposition_date	2006-03-09
Structure title title	GROEL-ADP-gp31 COMPLEX
Keywords keywords	CHAPERONIN, CHAPERONE, CELL CYCLE, CELL DIVISION, CAPSID ASSEMBLY, EARLY PROTEIN; CHAPERONE
Experimental Method method	ELECTRON MICROSCOPY

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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.

2cgt__assembly_1__model_1

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

Download this curve (.dat)

2cgt__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2cgt__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	69.18 Å
Rg (electron density)	69.11 Å
Total Rg	69.11 Å
Atom count	57953
Residues	7854
Excluded volume	1039900 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2cgt__assembly_1__model_1`	21-meric （21）	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 (2)

Entity 1 Entity 1 polymer

Description description	60 KDA GROEL
Molecular weight formula_weight	57260.5 kDa
Source method src_method	man
Copy count entity_count	14

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N
Atom count atom_count	57953

AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGMGGMGGMM

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	CAPSID ASSEMBLY PROTEIN 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	O,P,Q,R,S,T,U

MSEVQQLPIRAVGEYVILVSEPAQAGDEEVTESGLIIGKRVQGEVPELCVVHSVGPDVPEGFCEVGDLTSLPVGQIRNVPHPFVALGLKQPKEIKQKFVTCHYKAIPCLYK

Source Source

Source organism organism	BACTERIOPHAGE T4
NCBI taxonomy ID ncbi_taxonomy_id	10665
Host organism host_organism	ESCHERICHIA COLI

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

Domain ID domain_id	d2cgto1
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	d2cgtp1
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	d2cgtq1
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	d2cgtr1
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	d2cgts1
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	d2cgtt1
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	d2cgtu1
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

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

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

Resolution resolution	8.200 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	8.20 Å
Resolution测定Method resolution_method	PROJECTION MATCHING
颗粒数 num_particles	10300

GROEL-ADP-gp31 COMPLEX

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

60 KDA GROEL

State in the Current Structure

Other States of the Same Protein in the Database

CAPSID ASSEMBLY PROTEIN 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

2cgt__assembly_1__model_1

2cgt__assembly_1__model_1 | I(q)

2cgt__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

7. Citations (1)

GROEL-ADP-gp31 COMPLEX

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

60 KDA GROEL

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

CAPSID ASSEMBLY PROTEIN 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

2cgt__assembly_1__model_1

2cgt__assembly_1__model_1 | I(q)

2cgt__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

7. Citations (1)