1wr6

Crystal structure of GGA3 GAT domain in complex with ubiquitin

Method: X-RAY DIFFRACTION Dmax: 109.9 Å Quality: GOOD

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 209–319 Fragment:C-GAT domain(RESIDUES 209-319) Non-standard monomer:Yes (specific site not provided by mmCIF) ubiquitin × 1 (P62990) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;PEG3350, Ammonium formate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.290
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 209–319 Fragment:C-GAT domain(RESIDUES 209-319) Non-standard monomer:Yes (specific site not provided by mmCIF) ubiquitin × 1 (P62990) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;PEG3350, Ammonium formate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.290
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 209–319 Fragment:C-GAT domain(RESIDUES 209-319) Non-standard monomer:Yes (specific site not provided by mmCIF) ubiquitin × 1 (P62990) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;PEG3350, Ammonium formate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.290
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 209–319 Fragment:C-GAT domain(RESIDUES 209-319) Non-standard monomer:Yes (specific site not provided by mmCIF) ubiquitin × 1 (P62990) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;PEG3350, Ammonium formate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.290

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 24 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 1–111; UniProt 209–319 Author chain B; PDBConstruct 1–111; UniProt 209–319 Author chain C; PDBConstruct 1–111; UniProt 209–319 Author chain D; PDBConstruct 1–111; UniProt 209–319

ubiquitin

OrganismNot specified

UniProt P62990

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 1–76 Not recorded ADP-ribosylation factor binding protein GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;PEG3350, Ammonium formate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.290
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–76 Not recorded ADP-ribosylation factor binding protein GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;PEG3350, Ammonium formate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.290
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–76 Not recorded ADP-ribosylation factor binding protein GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;PEG3350, Ammonium formate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.290
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1–76 Not recorded ADP-ribosylation factor binding protein GGA3 × 1 (Q9NZ52) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;PEG3350, Ammonium formate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.60 Å R-free 0.290

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 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBIQ_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–76; UniProt 1–76 Author chain F; PDBConstruct 1–76; UniProt 1–76 Author chain G; PDBConstruct 1–76; UniProt 1–76 Author chain H; PDBConstruct 1–76; UniProt 1–76

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 1wr6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1wr6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1wr6
Deposition date deposition_date2004-10-12
Structure title titleCrystal structure of GGA3 GAT domain in complex with ubiquitin
Keywords keywordsthree-helix bundle, ubiquitin-binding protein, clathrin coat adaptor protein, PROTEIN TRANSPORT-SIGNALING PROTEIN COMPLEX; PROTEIN TRANSPORT/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.26
Radius of gyration Rg (electron density) rg_electron32.86
Forward intensity I(0) i094168100.00
Molecular weight molecular_weight74613.0 kDa
Excluded volume excluded_volume92389 ų
Envelope volume envelope_volume124120 ų
Hydration-shell volume shell_volume33208 ų
Envelope diameter envelope_diameter108.7
Shell Rg shell_rg37.74
Envelope Rg envelope_rg32.50
Shape Rg shape_rg32.87
Total Rg total_rg33.22
Total atoms total_atoms5209
Residues n_residues641
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 dmax109.9
Rg (real space) rg_real33.27
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real9.4170e+07
I(0) uncertainty (real space) i0_real_error1.5950e+06
Rg (reciprocal space) rg_reciprocal33.28
I(0) (reciprocal space) i0_reciprocal94170000.0000
Solution quality estimate total_estimate0.8959
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.5
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.605
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14240000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.933; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1wr6a1
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.8 — GAT-like domain
Family Family familya.7.8.1 — GAT domain
Domain ID domain_idd1wr6b_
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.8 — GAT-like domain
Family Family familya.7.8.1 — GAT domain
Domain ID domain_idd1wr6c_
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.8 — GAT-like domain
Family Family familya.7.8.1 — GAT domain
Domain ID domain_idd1wr6d_
Class classa — All alpha proteins
Fold Fold folda.7 — Spectrin repeat-like
Superfamily Superfamily superfamilya.7.8 — GAT-like domain
Family Family familya.7.8.1 — GAT domain
Domain ID domain_idd1wr6e_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd1wr6f_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd1wr6g_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd1wr6h_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related

CATH v4.4 (8 domains)

Domain ID domain_id1wr6A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily160
Domain ID domain_id1wr6B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily160
Domain ID domain_id1wr6C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily160
Domain ID domain_id1wr6D00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily160
Domain ID domain_id1wr6E00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id1wr6F00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id1wr6G00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id1wr6H00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)