3g2t

VHS Domain of human GGA1 complexed with SorLA C-terminal Phosphopeptide

Method: X-RAY DIFFRACTION Dmax: 61.0 Å Quality: EXCELLENT

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

ADP-ribosylation factor-binding protein GGA1

Homo sapiens

UniProt Q9UJY5

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 1–147 Fragment:VHS Domain (N-terminal domain) Phosphorylated C-terminal fragment of Sortilin-related receptor × 1 (Q92673) IOD IODIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;292 K;18%(w/v) PEG 5000 MME, 0.2M NH4I, 0.1M TRIS-HCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.00 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–147 Fragment:VHS Domain (N-terminal domain) Phosphorylated C-terminal fragment of Sortilin-related receptor × 1 (Q92673) IOD IODIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;292 K;18%(w/v) PEG 5000 MME, 0.2M NH4I, 0.1M TRIS-HCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.00 Å R-free 0.233

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.

19 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GGA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–149; UniProt 1–147 Author chain B; PDBConstruct 3–149; UniProt 1–147

Phosphorylated C-terminal fragment of Sortilin-related receptor

OrganismNot specified

UniProt Q92673

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 C; UniProt 2202–2214 Non-standard monomer:Yes (specific site not provided by mmCIF) ADP-ribosylation factor-binding protein GGA1 × 1 (Q9UJY5) IOD IODIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;292 K;18%(w/v) PEG 5000 MME, 0.2M NH4I, 0.1M TRIS-HCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.00 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2202–2214 Non-standard monomer:Yes (specific site not provided by mmCIF) ADP-ribosylation factor-binding protein GGA1 × 1 (Q9UJY5) IOD IODIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;292 K;18%(w/v) PEG 5000 MME, 0.2M NH4I, 0.1M TRIS-HCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.00 Å R-free 0.233

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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SORL_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–13; UniProt 2202–2214 Author chain D; PDBConstruct 1–13; UniProt 2202–2214

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 3g2t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3g2t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3g2t
Deposition date deposition_date2009-02-01
Structure title titleVHS Domain of human GGA1 complexed with SorLA C-terminal Phosphopeptide
Keywords keywordsADP-ribosylation factor binding protein GGA1, VHS, acidic-cluster dileucine signal, SorLA, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.48
Radius of gyration Rg (electron density) rg_electron19.45
Forward intensity I(0) i022454500.00
Molecular weight molecular_weight34935.0 kDa
Excluded volume excluded_volume43067 ų
Envelope volume envelope_volume50165 ų
Hydration-shell volume shell_volume21388 ų
Envelope diameter envelope_diameter61.9
Shell Rg shell_rg25.83
Envelope Rg envelope_rg19.49
Shape Rg shape_rg19.42
Total Rg total_rg20.36
Total atoms total_atoms2389
Residues n_residues295
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 dmax61.0
Rg (real space) rg_real20.37
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.2450e+07
I(0) uncertainty (real space) i0_real_error2.5510e+05
Rg (reciprocal space) rg_reciprocal20.39
I(0) (reciprocal space) i0_reciprocal22450000.0000
Solution quality estimate total_estimate0.9079
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.157
Kurtosis Kurtosis kurtosis-0.516
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4251000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3g2ta_
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_idd3g2tb_
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

CATH v4.4 (2 domains)

Domain ID domain_id3g2tA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily90
Domain ID domain_id3g2tB00
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)