SAXSdb — 9x41

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

Proto-oncogene Mas

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 R； UniProt 1–325	Not recorded	A1MCH 1-(4-fluorophenyl)-4-[[(3~{R},4~{R})-4-(3-fluorophenyl)-1-(2-methoxy-4-nitro-phenyl)sulfonyl-pyrrolidin-3-yl]methyl]piperazine × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.31 Å

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 9X41	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
25IK Cryo-EM structure of MasR(FL)-Gq Deposited 2026-04-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 2–325（324 aa）	Mutation：M29W/H124I	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
25IL Cryo-EM structure of MasR(del2-25)-Gq Deposited 2026-04-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 26–325（300 aa）	Mutation：M29W,H124I	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9JLC Cryo-EM structure of MAS1-Gi Complex with AVE 0991 Deposited 2024-09-18	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 31–283（253 aa）	Not recorded	A1ECD 1-ethyl-3-[3-[4-[(5-methanoyl-4-methoxy-2-phenyl-imidazol-1-yl)methyl]phenyl]-5-(2-methylpropyl)thiophen-2-yl]sulfonyl-urea × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.98 Å
9X3Y NPFF bound Mas1 Receptor Deposited 2025-10-09	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain R 1–325（325 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.77 Å
9X3Z NPFF bound Mas1 Receptor Complex Deposited 2025-10-09	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 1–325（325 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.54 Å
9X40 AR234958 bound Mas1 Receptor Complex Deposited 2025-10-09	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–325（325 aa）	Not recorded	A1MCH 1-(4-fluorophenyl)-4-[[(3~{R},4~{R})-4-(3-fluorophenyl)-1-(2-methoxy-4-nitro-phenyl)sulfonyl-pyrrolidin-3-yl]methyl]piperazine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MAS_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain R； PDBConstruct 1–325； UniProt 1–325

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	9x41
Deposition date deposition_date	2025-10-09
Structure title title	AR234958 bound Mas1 Receptor
Keywords keywords	GPCR, Agonist, Orphan Receptor..., PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	19.95 Å
Radius of gyration Rg (electron density) rg_electron	19.13 Å
Forward intensity I(0) i0	23318000.00
Molecular weight molecular_weight	26444.0 kDa
Excluded volume excluded_volume	26588 Å³
Envelope volume envelope_volume	42780 Å³
Hydration-shell volume shell_volume	18917 Å³
Envelope diameter envelope_diameter	68.4 Å
Shell Rg shell_rg	25.29 Å
Envelope Rg envelope_rg	19.61 Å
Shape Rg shape_rg	19.12 Å
Total Rg total_rg	19.88 Å
Total atoms total_atoms	2012
Residues n_residues	242
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	69.3 Å
Rg (real space) rg_real	19.94 Å
Rg uncertainty (real space) rg_real_error	0.40 Å
I(0) (real space) i0_real	2.3320e+07
I(0) uncertainty (real space) i0_real_error	3.2560e+05
Rg (reciprocal space) rg_reciprocal	19.94 Å
I(0) (reciprocal space) i0_reciprocal	23320000.0000
Solution quality estimate total_estimate	0.8624
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	23.4 Å
Skewness Skewness skewness	0.374
Kurtosis Kurtosis kurtosis	-0.230
Angular range angular_range	— – 0.4000 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	3303000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.755; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.995

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Proto-oncogene Mas
Molecular weight formula_weight	37502.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	R
Atom count atom_count	2012

MDGSNVTSFVVEEPTNISTGRNASVGNAHRQIPIVHWVIMSISPVGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKYQSALVCALLWALSCLVTTMEYVMCIDREEESHSRNDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRLLYLLYYEYWSTFGNLHHISLLFSTINSSANPFIYFFVGSSKKKRFKESLKVVLTRAFKDEMQPRRQKDNCNTVTVETVV

来源 Source

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	Spodoptera frugiperda

Entity 2 Entity 2 non-polymer

Description description	1-(4-fluorophenyl)-4-[[(3~{R},4~{R})-4-(3-fluorophenyl)-1-(2-methoxy-4-nitro-phenyl)sulfonyl-pyrrolidin-3-yl]methyl]piperazine
Molecular weight formula_weight	572.6 kDa
Source method src_method	syn
Copy count entity_count	1

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8. Citations (1)

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

Resolution resolution	3.31 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	162204

fit	/app/data/saxs_computation/x4/9x41/9x41.fit
pddf	/app/data/pr_computation/x4/9x41/9x41.pr.out
profile	/app/data/saxs_computation/x4/9x41/9x41.dat

AR234958 bound Mas1 Receptor

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

Proto-oncogene Mas

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

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)