1o3x

Crystal structure of human GGA1 GAT domain

Method: X-RAY DIFFRACTION Dmax: 75.3 Å Quality: REASONABLE

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 166–305 Fragment:Gat domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;MPD, PEG6000, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.10 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 39 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 1–140; UniProt 166–305

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 1o3x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1o3x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1o3x
Deposition date deposition_date2003-05-08
Structure title titleCrystal structure of human GGA1 GAT domain
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_guinier18.98
Radius of gyration Rg (electron density) rg_electron18.96
Forward intensity I(0) i03579050.00
Molecular weight molecular_weight12717.0 kDa
Excluded volume excluded_volume15663 ų
Envelope volume envelope_volume20568 ų
Hydration-shell volume shell_volume10749 ų
Envelope diameter envelope_diameter75.3
Shell Rg shell_rg22.21
Envelope Rg envelope_rg20.24
Shape Rg shape_rg18.92
Total Rg total_rg19.65
Total atoms total_atoms886
Residues n_residues112
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 dmax75.3
Rg (real space) rg_real19.40
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real3.5790e+06
I(0) uncertainty (real space) i0_real_error4.7850e+04
Rg (reciprocal space) rg_reciprocal19.33
I(0) (reciprocal space) i0_reciprocal3579000.0000
Solution quality estimate total_estimate0.6863
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.7
Skewness Skewness skewness0.806
Kurtosis Kurtosis kurtosis0.309
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha720800.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.270; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.111; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1o3xa_
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 (1 domains)

Domain ID domain_id1o3xA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily160

8. Citations (1)

9. Files and Curves (10)