SAXSdb — 6vu8

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

Resistance to inhibitors of cholinesterase 8 homolog A (C. elegans)

Rattus norvegicus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Guanine nucleotide-binding protein G(i) subunit alpha-1 × 1 （P63096）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	B1H241_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–534； UniProt 1–530

Guanine nucleotide-binding protein G(i) subunit alpha-1

Homo sapiens

UniProt P63096

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Resistance to inhibitors of cholinesterase 8 homolog A (C. elegans) × 1 （B1H241）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GNAI1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–359； UniProt 2–354

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	6vu8
Deposition date deposition_date	2020-02-14
Structure title title	Structure of G-alpha-i bound to its chaperone Ric-8A
Keywords keywords	;G protein alpha subunit, Ric-8; molecular chaperone; G alpha folding; guanine nucleotide exchange factor (GEF); cryoEM structure; protein complex; G protein-coupled receptor (GPCR), phosphorylation; quality control., CHAPERONE ;; 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.

6vu8__assembly_1__model_1

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

Download this curve (.dat)

6vu8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6vu8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	31.77 Å
Rg (electron density)	30.94 Å
Total Rg	31.42 Å
Atom count	5249
Residues	667
Excluded volume	93413 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6vu8__assembly_1__model_1`	dimeric （2）	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	Resistance to inhibitors of cholinesterase 8 homolog A (C. elegans)
Molecular weight formula_weight	60512.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5249

QGEFMEPRAVADALETGEEDAVTEALRSFNREHSQSFTFDDAQQEDRKRLAKLLVSVLEQGLSPKHRVTWLQTIRILSRDRSCLDSFASRQSLHALACYADIAISEEPIPQPPDMDVLLESLKCLCNLVLSSPTAQMLAAEARLVVRLAERVGLYRKRSYPHEVQFFDLRLLFLLTALRTDVRQQLFQELHGVRLLTDALELTLGVAPKENPLVILPAQETERAMEILKVLFNITFDSVKREVDEEDAALYRYLGTLLRHCVMADAAGDRTEEFHGHTVNLLGNLPLKCLDVLLALELHEGSLEFMGVNMDVINALLAFLEKRLHQTHRLKECVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGDLLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTEEYREAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVNMFDKLSRHRLIQPMGMSPRGHLTSLQDAMCETMEGQLSSDPDSDPD

Source Source

Source organism organism	Rattus norvegicus
Common name common_name	Rat
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	Trichoplusia ni

Entity 2 Entity 2 polymer

Description description	Guanine nucleotide-binding protein G(i) subunit alpha-1
Molecular weight formula_weight	41112.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMHHHHHHTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

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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	—

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

Resolution resolution	4.14 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	153110

Structure of G-alpha-i bound to its chaperone Ric-8A

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

Resistance to inhibitors of cholinesterase 8 homolog A (C. elegans)

State in the Current Structure

Other States of the Same Protein in the Database

Guanine nucleotide-binding protein G(i) subunit alpha-1

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

6vu8__assembly_1__model_1

6vu8__assembly_1__model_1 | I(q)

6vu8__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

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

7. Citations (1)

Structure of G-alpha-i bound to its chaperone Ric-8A

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

Resistance to inhibitors of cholinesterase 8 homolog A (C. elegans)

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Guanine nucleotide-binding protein G(i) subunit alpha-1

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

6vu8__assembly_1__model_1

6vu8__assembly_1__model_1 | I(q)

6vu8__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

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

7. Citations (1)