9w3k

GPR151-Legobody complex

Method: ELECTRON MICROSCOPY Dmax: 164.6 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

;Streptococcus sp. 'group G' ;

UniProt P06654

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 295–352 Not recorded Fab-8D3-2-H-His × 1 Fab_8D3_L × 1 G-protein coupled receptor 151 × 1 (Q8TDV0) NB6 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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.

48 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPG1_STRSG
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 499–556; UniProt 295–352

Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

;Streptococcus sp. 'group G' ;

UniProt P0A015

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 103–151 Not recorded Fab-8D3-2-H-His × 1 Fab_8D3_L × 1 G-protein coupled receptor 151 × 1 (Q8TDV0) NB6 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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.

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

View Construct and Data Evidence
UniProt name SPA_STAAM
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 439–487; UniProt 103–151

Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

;Streptococcus sp. 'group G' ;

UniProt P0AEY0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 27–394 Not recorded Fab-8D3-2-H-His × 1 Fab_8D3_L × 1 G-protein coupled receptor 151 × 1 (Q8TDV0) NB6 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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.

109 other PDB entries and 148 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 22–389; UniProt 27–394

Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

;Streptococcus sp. 'group G' ;

UniProt P38507

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 289–327 Not recorded Fab-8D3-2-H-His × 1 Fab_8D3_L × 1 G-protein coupled receptor 151 × 1 (Q8TDV0) NB6 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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.

66 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 391–429; UniProt 289–327

G-protein coupled receptor 151

Homo sapiens

UniProt Q8TDV0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–221 Chain A; UniProt 253–419 Not recorded Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G × 1 (P0AEY0,P38507,P0A015,P06654) Fab-8D3-2-H-His × 1 Fab_8D3_L × 1 NB6 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP151_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–221; UniProt 1–221 Author chain A; PDBConstruct 253–419; UniProt 253–419

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 9w3k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9w3k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9w3k
Deposition date deposition_date2025-07-29
Structure title titleGPR151-Legobody complex
Keywords keywordsorphan GPCR, cryo-EM, Legobody, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.83
Radius of gyration Rg (electron density) rg_electron50.97
Forward intensity I(0) i0243540000.00
Molecular weight molecular_weight132090.0 kDa
Excluded volume excluded_volume166610 ų
Envelope volume envelope_volume254690 ų
Hydration-shell volume shell_volume45583 ų
Envelope diameter envelope_diameter163.5
Shell Rg shell_rg47.49
Envelope Rg envelope_rg50.52
Shape Rg shape_rg51.01
Total Rg total_rg50.69
Total atoms total_atoms9329
Residues n_residues1222
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax164.6
Rg (real space) rg_real50.13
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real2.4350e+08
I(0) uncertainty (real space) i0_real_error5.0200e+06
Rg (reciprocal space) rg_reciprocal49.84
I(0) (reciprocal space) i0_reciprocal243400000.0000
Solution quality estimate total_estimate0.8307
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.9
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.846
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13330000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.753; Smooth: 0.548

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)