1j2j

Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 GTP form

Method: X-RAY DIFFRACTION Dmax: 58.7 Å Quality: GOOD

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

ADP-ribosylation factor 1

Mus musculus

UniProt Q8BSL7

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 18–181 Fragment:residues 18-181 Mutation:Q71L ADP-ribosylation factor binding protein GGA1 × 1 (Q9UJY5) MG MAGNESIUM ION × 1 IOD IODIDE ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;PEG3350, KI, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.60 Å R-free 0.227

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 ARF2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–166; UniProt 18–181

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 B; UniProt 166–210 Fragment:GAT N-terminal region ADP-ribosylation factor 1 × 1 (Q8BSL7) MG MAGNESIUM ION × 1 IOD IODIDE ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;PEG3350, KI, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.60 Å R-free 0.227

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 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GGA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–45; UniProt 166–210

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 1j2j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1j2j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1j2j
Deposition date deposition_date2003-01-05
Structure title titleCrystal structure of GGA1 GAT N-terminal region in complex with ARF1 GTP form
Keywords keywordsPROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.35
Radius of gyration Rg (electron density) rg_electron16.94
Forward intensity I(0) i011820300.00
Molecular weight molecular_weight24451.0 kDa
Excluded volume excluded_volume30091 ų
Envelope volume envelope_volume35234 ų
Hydration-shell volume shell_volume17253 ų
Envelope diameter envelope_diameter59.1
Shell Rg shell_rg23.23
Envelope Rg envelope_rg17.43
Shape Rg shape_rg16.90
Total Rg total_rg18.01
Total atoms total_atoms1696
Residues n_residues206
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 dmax58.7
Rg (real space) rg_real18.24
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real1.1820e+07
I(0) uncertainty (real space) i0_real_error1.3530e+05
Rg (reciprocal space) rg_reciprocal18.26
I(0) (reciprocal space) i0_reciprocal11820000.0000
Solution quality estimate total_estimate0.8149
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.150
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1613000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1j2ja1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1j2ja2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1j2jb_
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

CATH v4.4 (2 domains)

Domain ID domain_id1j2jA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1j2jB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170

8. Citations (1)

9. Files and Curves (10)