SAXSdb — 1mot

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

Glycine Receptor alpha-1 CHAIN

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 277–304	Fragment：Extented second transmembrane domain	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5；303 K；Ionic strength (raw mmCIF value) 300 mM SDS concentration；Pressure 1 NMR sample composition：SDS concentration: 300 mM Peptide concentration: 2 mM \| 90% H2O/10% D2O	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1MOT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1VRY Second and Third Transmembrane Domains of the Alpha-1 Subunit of Human Glycine Receptor Deposited 2005-07-20	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 278–337（60 aa） Fragment：SECOND AND THIRD TRANSMEMBRANE DOMAINS	Mutation：YES	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Pressure 1 NMR sample composition 1MM TM23 U-15N, TRIFLUOROETHANOL-D2; 1MM TM23 U-15N,13C, TRIFLUOROETHANOL-D2	Resolution not provided
8DN2 Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state 2(expanded open) Deposited 2022-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 29–457（429 aa） Chain B 29–457（429 aa） Chain C 29–457（429 aa） Chain D 29–457（429 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 HEX HEXANE × 10 HP6 HEPTANE × 9 UND UNDECANE × 3 OCT N-OCTANE × 7 GLY GLYCINE × 3 DD9 nonane × 2 NBU N-BUTANE × 3 D10 DECANE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
8DN3 Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, apo state Deposited 2022-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 29–457（429 aa） Chain B 29–457（429 aa） Chain C 29–457（429 aa） Chain D 29–457（429 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 HEX HEXANE × 15 UND UNDECANE × 12 DD9 nonane × 13 NBU N-BUTANE × 5 HP6 HEPTANE × 8 D10 DECANE × 1 CL CHLORIDE ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.55 Å
8DN4 Cryo-EM structure of human Glycine Receptor alpha-1 beta heteromer, glycine-bound state3(desensitized state) Deposited 2022-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 29–457（429 aa） Chain B 29–457（429 aa） Chain C 29–457（429 aa） Chain D 29–457（429 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 LNK PENTANE × 1 HEX HEXANE × 9 NBU N-BUTANE × 3 OCT N-OCTANE × 1 DD9 nonane × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
8DN5 Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state1(open state) Deposited 2022-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 29–457（429 aa） Chain B 29–457（429 aa） Chain C 29–457（429 aa） Chain D 29–457（429 aa）	Not recorded	GLY GLYCINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 DD9 nonane × 4 HP6 HEPTANE × 6 HEX HEXANE × 13 UND UNDECANE × 6 NBU N-BUTANE × 8 D10 DECANE × 3 OCT N-OCTANE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.63 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GLRA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–28； UniProt 277–304

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	1mot
Deposition date deposition_date	2002-09-09
Structure title title	NMR Structure Of Extended Second Transmembrane Domain Of Glycine Receptor alpha1 Subunit in SDS Micelles
Keywords keywords	glycine receptor, second transmembrane domain, micelles, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	SOLUTION NMR

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	11.62 Å
Radius of gyration Rg (electron density) rg_electron	11.64 Å
Forward intensity I(0) i0	48724500.00
Molecular weight molecular_weight	56086.0 kDa
Excluded volume excluded_volume	70411 Å³
Envelope volume envelope_volume	21443 Å³
Hydration-shell volume shell_volume	12302 Å³
Envelope diameter envelope_diameter	49.9 Å
Shell Rg shell_rg	20.34 Å
Envelope Rg envelope_rg	15.50 Å
Shape Rg shape_rg	11.63 Å
Total Rg total_rg	12.29 Å
Total atoms total_atoms	8160
Residues n_residues	560
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	29.9 Å
Rg (real space) rg_real	10.95 Å
Rg uncertainty (real space) rg_real_error	0.04 Å
I(0) (real space) i0_real	4.6570e+07
I(0) uncertainty (real space) i0_real_error	3.4480e+05
Rg (reciprocal space) rg_reciprocal	11.77 Å
I(0) (reciprocal space) i0_reciprocal	48720000.0000
Solution quality estimate total_estimate	0.6658
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	13.6 Å
Skewness Skewness skewness	0.144
Kurtosis Kurtosis kurtosis	-0.835
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	4.6390
Highest regularization parameter α highest_alpha	5680.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.999; Stabil: 0.975; Sysdev: 0.000; Positv: 1.000; Valcen: 0.733; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1mota_
Class class	j — Peptides
Fold Fold fold	j.35 — Transmembrane helical fragments
Superfamily Superfamily superfamily	j.35.1 — Transmembrane helical fragments
Family Family family	j.35.1.1 — Transmembrane helical fragments

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8. Citations (1)

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Description description	Glycine Receptor alpha-1 CHAIN
Molecular weight formula_weight	2804.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	8160

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21

fit	/app/data/saxs_computation/mo/1mot/1mot.fit
pddf	/app/data/pr_computation/mo/1mot/1mot.pr.out
profile	/app/data/saxs_computation/mo/1mot/1mot.dat

NMR Structure Of Extended Second Transmembrane Domain Of Glycine Receptor alpha1 Subunit in SDS Micelles

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

Glycine Receptor alpha-1 CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)