1nwm

GAT domain of human GGA1

Method: X-RAY DIFFRACTION Dmax: 50.8 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 X; UniProt 166–302 Fragment:GAT domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.2;298.15 K;polyethylene glycol 4000, iso-propanol, sodium citrate, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.15K Resolution 2.40 Å R-free 0.286

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 X; PDBConstruct 6–142; UniProt 166–302

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 1nwm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1nwm
Deposition date deposition_date2003-02-06
Structure title titleGAT domain of human GGA1
Keywords keywordsthree-alpha helical bundle, 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_guinier18.84
Radius of gyration Rg (electron density) rg_electron19.07
Forward intensity I(0) i03310160.00
Molecular weight molecular_weight12248.0 kDa
Excluded volume excluded_volume15143 ų
Envelope volume envelope_volume19612 ų
Hydration-shell volume shell_volume10444 ų
Envelope diameter envelope_diameter75.8
Shell Rg shell_rg21.83
Envelope Rg envelope_rg20.05
Shape Rg shape_rg19.02
Total Rg total_rg19.73
Total atoms total_atoms853
Residues n_residues105
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 dmax50.8
Rg (real space) rg_real17.31
Rg uncertainty (real space) rg_real_error0.12
I(0) (real space) i0_real3.1480e+06
I(0) uncertainty (real space) i0_real_error3.0180e+04
Rg (reciprocal space) rg_reciprocal19.19
I(0) (reciprocal space) i0_reciprocal3310000.0000
Solution quality estimate total_estimate0.6716
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.9
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis-0.471
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha2.2510
Highest regularization parameter α highest_alpha512900.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.939; Stabil: 0.993; Sysdev: 0.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.000

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_idd1nwmx_
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_id1nwmX00
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)