1naf

Crystal structure of the human GGA1 GAT domain

Method: X-RAY DIFFRACTION Dmax: 83.6 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 165–314 Fragment:GAT domain, Residues 165-314 of SWS Q9UJY5 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;289 K;sodium acetate, lithium sulphate, NaH2PO4/K2HPO4, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.80 Å R-free 0.283

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 9–158; UniProt 165–314

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 1naf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1naf
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1naf
Deposition date deposition_date2002-11-27
Structure title titleCrystal structure of the human GGA1 GAT domain
Keywords keywordsclathrin-adaptor, GGA, GAT domain, helical paper-clip, three-helix bundle, SIGNALING PROTEIN, MEMBRANE PROTEIN; SIGNALING PROTEIN, MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.79
Radius of gyration Rg (electron density) rg_electron23.05
Forward intensity I(0) i04812630.00
Molecular weight molecular_weight14778.0 kDa
Excluded volume excluded_volume17945 ų
Envelope volume envelope_volume24036 ų
Hydration-shell volume shell_volume10904 ų
Envelope diameter envelope_diameter83.4
Shell Rg shell_rg25.02
Envelope Rg envelope_rg23.60
Shape Rg shape_rg23.03
Total Rg total_rg23.40
Total atoms total_atoms1006
Residues n_residues117
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 dmax83.6
Rg (real space) rg_real23.34
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real4.8130e+06
I(0) uncertainty (real space) i0_real_error7.8860e+04
Rg (reciprocal space) rg_reciprocal23.21
I(0) (reciprocal space) i0_reciprocal4812000.0000
Solution quality estimate total_estimate0.6809
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.5
Skewness Skewness skewness0.710
Kurtosis Kurtosis kurtosis-0.268
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha584700.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.280; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.068; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1nafa_
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_id1nafA01
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
Domain ID domain_id1nafA02
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)