SAXSdb — 6d1s

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

chimeric alpha1GABAA receptor

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 5	No other associated polymer	Consistent with protein count
2	Insufficient information	Homooligomer	Protein 5	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	E0SJQ4_DICD3
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–199； UniProt 22–220 Author chain B； PDBConstruct 1–199； UniProt 22–220 Author chain C； PDBConstruct 1–199； UniProt 22–220 Author chain D； PDBConstruct 1–199； UniProt 22–220 Author chain E； PDBConstruct 1–199； UniProt 22–220 Author chain F； PDBConstruct 1–199； UniProt 22–220 Author chain G； PDBConstruct 1–199； UniProt 22–220 Author chain H； PDBConstruct 1–199； UniProt 22–220 Author chain I； PDBConstruct 1–199； UniProt 22–220 Author chain J； PDBConstruct 1–199； UniProt 22–220

chimeric alpha1GABAA receptor

Homo sapiens

UniProt P14867

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 5	No other associated polymer	Consistent with protein count
2	Insufficient information	Homooligomer	Protein 5	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GBRA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 200–291； UniProt 249–340 Author chain A； PDBConstruct 295–324； UniProt 415–444 Author chain B； PDBConstruct 200–291； UniProt 249–340 Author chain B； PDBConstruct 295–324； UniProt 415–444 Author chain C； PDBConstruct 200–291； UniProt 249–340 Author chain C； PDBConstruct 295–324； UniProt 415–444 Author chain D； PDBConstruct 200–291； UniProt 249–340 Author chain D； PDBConstruct 295–324； UniProt 415–444 Author chain E； PDBConstruct 200–291； UniProt 249–340 Author chain E； PDBConstruct 295–324； UniProt 415–444 Author chain F； PDBConstruct 200–291； UniProt 249–340 Author chain F； PDBConstruct 295–324； UniProt 415–444 Author chain G； PDBConstruct 200–291； UniProt 249–340 Author chain G； PDBConstruct 295–324； UniProt 415–444 Author chain H； PDBConstruct 200–291； UniProt 249–340 Author chain H； PDBConstruct 295–324； UniProt 415–444 Author chain I； PDBConstruct 200–291； UniProt 249–340 Author chain I； PDBConstruct 295–324； UniProt 415–444 Author chain J； PDBConstruct 200–291； UniProt 249–340 Author chain J； PDBConstruct 295–324； UniProt 415–444

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	6d1s
Deposition date deposition_date	2018-04-12
Structure title title	Crystal structure of an apo chimeric human alpha1GABAA receptor
Keywords keywords	GABAA receptor, anesthetics, alphaxalone, neurosteroids, PROTEIN TRANSPORT; PROTEIN TRANSPORT
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.

6d1s__assembly_1__model_1

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

Download this curve (.dat)

6d1s__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6d1s__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	37.76 Å
Rg (electron density)	37.07 Å
Total Rg	37.62 Å
Atom count	12845
Residues	1570
Excluded volume	230520 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6d1s__assembly_1__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6d1s__assembly_2__model_1`	pentameric （5）	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 (1)

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6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id	6d1sA01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sB01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sC01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sD01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sE01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sF01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sG01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sH01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sI01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	6d1sJ01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

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Unit-cell length a length_a	108.517 Å
Unit-cell length b length_b	264.846 Å
Unit-cell length c length_c	109.153 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	110.46 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

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

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	37.766 Å
R factor r_factor	0.2224
R_work r_work	0.2200
R_free r_free	0.2689

Description description	chimeric alpha1GABAA receptor
Molecular weight formula_weight	37225.4 kDa
Source method src_method	man
Copy count entity_count	10

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	25690

Crystal structure of an apo chimeric human alpha1GABAA receptor

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

chimeric alpha1GABAA receptor

State in the Current Structure

Other States of the Same Protein in the Database

chimeric alpha1GABAA receptor

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

6d1s__assembly_1__model_1

6d1s__assembly_1__model_1 | I(q)

6d1s__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

7. Citations (1)

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

Crystal structure of an apo chimeric human alpha1GABAA receptor

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

chimeric alpha1GABAA receptor

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

chimeric alpha1GABAA receptor

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

6d1s__assembly_1__model_1

6d1s__assembly_1__model_1 | I(q)

6d1s__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

7. Citations (1)