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9x3y

NPFF bound Mas1 Receptor

Method: ELECTRON MICROSCOPY Dmax: 64.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Proto-oncogene Mas

Homo sapiens

UniProt P04201

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain R； UniProt 1–325 Not recorded NPFF × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.77 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 9X3Y 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 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 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
9X3Z NPFF bound Mas1 Receptor Complex Deposited 2025-10-09 Different oligomeric state 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 ligand/ion 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
9X41 AR234958 bound Mas1 Receptor Deposited 2025-10-09 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
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 3.31 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.

SAXS scattering curve SAXS Profile

SAXS profile for 9x3y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x3y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x3y
Deposition date deposition_date2025-10-09
Structure title titleNPFF bound Mas1 Receptor
Keywords keywordsGPCR, Agonist, Orphan Receptor, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.78 Å
Radius of gyration Rg (electron density) rg_electron18.84 Å
Forward intensity I(0) i011028400.00
Molecular weight molecular_weight28534.0 kDa
Excluded volume excluded_volume37273 ų
Envelope volume envelope_volume41514 ų
Hydration-shell volume shell_volume18631 ų
Envelope diameter envelope_diameter67.5 Å
Shell Rg shell_rg25.04 Å
Envelope Rg envelope_rg19.27 Å
Shape Rg shape_rg18.84 Å
Total Rg total_rg19.86 Å
Total atoms total_atoms2015
Residues n_residues247
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax64.8 Å
Rg (real space) rg_real19.78 Å
Rg uncertainty (real space) rg_real_error0.44 Å
I(0) (real space) i0_real1.1030e+07
I(0) uncertainty (real space) i0_real_error1.4890e+05
Rg (reciprocal space) rg_reciprocal19.78 Å
I(0) (reciprocal space) i0_reciprocal11030000.0000
Solution quality estimate total_estimate0.8083
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7 Å
Skewness Skewness skewness0.361
Kurtosis Kurtosis kurtosis-0.266
Angular range angular_range— – 0.4000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1666000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)