1juq

GGA3 VHS domain complexed with C-terminal peptide from cation-dependent Mannose 6-phosphate receptor

Method: X-RAY DIFFRACTION Dmax: 88.4 Å Quality: EXCELLENT

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

ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3

Homo sapiens

UniProt Q9NZ52

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 A; UniProt 1–166 Fragment:VHS domain Non-standard monomer:Yes (specific site not provided by mmCIF) Cation-dependent mannose-6-phosphate receptor × 1 (P20645) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–166 Fragment:VHS domain Non-standard monomer:Yes (specific site not provided by mmCIF) Cation-dependent mannose-6-phosphate receptor × 1 (P20645) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–166 Fragment:VHS domain Non-standard monomer:Yes (specific site not provided by mmCIF) Cation-dependent mannose-6-phosphate receptor × 1 (P20645) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–166 Fragment:VHS domain Non-standard monomer:Yes (specific site not provided by mmCIF) Cation-dependent mannose-6-phosphate receptor × 1 (P20645) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
5 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–166 Chain B; UniProt 1–166 Chain C; UniProt 1–166 Chain D; UniProt 1–166 Fragment:VHS domain Non-standard monomer:Yes (specific site not provided by mmCIF) Cation-dependent mannose-6-phosphate receptor × 4 (P20645) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
6 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–166 Chain B; UniProt 1–166 Chain C; UniProt 1–166 Chain D; UniProt 1–166 Fragment:VHS domain Non-standard monomer:Yes (specific site not provided by mmCIF) Cation-dependent mannose-6-phosphate receptor × 2 (P20645) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254

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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GGA3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–171; UniProt 1–166 Author chain B; PDBConstruct 6–171; UniProt 1–166 Author chain C; PDBConstruct 6–171; UniProt 1–166 Author chain D; PDBConstruct 6–171; UniProt 1–166

Cation-dependent mannose-6-phosphate receptor

OrganismNot specified

UniProt P20645

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 E; UniProt 265–277 Fragment:C-terminal peptide ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 265–277 Fragment:C-terminal peptide ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 265–277 Fragment:C-terminal peptide ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 265–277 Fragment:C-terminal peptide ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
5 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 265–277 Chain F; UniProt 265–277 Chain G; UniProt 265–277 Chain H; UniProt 265–277 Fragment:C-terminal peptide ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 × 4 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254
6 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 265–277 Chain G; UniProt 265–277 Fragment:C-terminal peptide ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 × 4 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium/Potassium phosphate, Lithium Sulfate, CAPS, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.254

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name MPRD_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–13; UniProt 265–277 Author chain F; PDBConstruct 1–13; UniProt 265–277 Author chain G; PDBConstruct 1–13; UniProt 265–277 Author chain H; PDBConstruct 1–13; UniProt 265–277

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 1juq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1juq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1juq
Deposition date deposition_date2001-08-26
Structure title titleGGA3 VHS domain complexed with C-terminal peptide from cation-dependent Mannose 6-phosphate receptor
Keywords keywordsprotein-peptide complex; VHS domain; dxxll sorting signal, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.95
Radius of gyration Rg (electron density) rg_electron27.96
Forward intensity I(0) i090996000.00
Molecular weight molecular_weight74815.0 kDa
Excluded volume excluded_volume93540 ų
Envelope volume envelope_volume117010 ų
Hydration-shell volume shell_volume34634 ų
Envelope diameter envelope_diameter89.4
Shell Rg shell_rg35.48
Envelope Rg envelope_rg27.74
Shape Rg shape_rg27.98
Total Rg total_rg28.67
Total atoms total_atoms5214
Residues n_residues629
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 dmax88.4
Rg (real space) rg_real28.83
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real9.1000e+07
I(0) uncertainty (real space) i0_real_error1.0620e+06
Rg (reciprocal space) rg_reciprocal28.88
I(0) (reciprocal space) i0_reciprocal91000000.0000
Solution quality estimate total_estimate0.9113
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14200000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1juqa_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.9 — ENTH/VHS domain
Family Family familya.118.9.2 — VHS domain
Domain ID domain_idd1juqb1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.9 — ENTH/VHS domain
Family Family familya.118.9.2 — VHS domain
Domain ID domain_idd1juqb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1juqc_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.9 — ENTH/VHS domain
Family Family familya.118.9.2 — VHS domain
Domain ID domain_idd1juqd1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.9 — ENTH/VHS domain
Family Family familya.118.9.2 — VHS domain
Domain ID domain_idd1juqd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id1juqA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily90
Domain ID domain_id1juqB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily90
Domain ID domain_id1juqC00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily90
Domain ID domain_id1juqD00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily90

8. Citations (1)

9. Files and Curves (10)