1na8

Crystal structure of ADP-ribosylation factor binding protein GGA1

Method: X-RAY DIFFRACTION Dmax: 81.9 Å Quality: GOOD

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 494–639 Chain B; UniProt 494–639 Fragment:appendage domain, Residues 494-639 of SWS Q9UJY5 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;289 K;sodium citrate, ammonium sulphate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 289K Resolution 2.30 Å R-free 0.279

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 9–154; UniProt 494–639 Author chain B; PDBConstruct 9–154; UniProt 494–639

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 1na8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1na8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1na8
Deposition date deposition_date2002-11-27
Structure title titleCrystal structure of ADP-ribosylation factor binding protein GGA1
Keywords keywordsclathrin-adaptor, GGA, appendage, beta-sandwich, 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_guinier23.24
Radius of gyration Rg (electron density) rg_electron22.35
Forward intensity I(0) i017210500.00
Molecular weight molecular_weight33012.0 kDa
Excluded volume excluded_volume42138 ų
Envelope volume envelope_volume50847 ų
Hydration-shell volume shell_volume20071 ų
Envelope diameter envelope_diameter82.6
Shell Rg shell_rg28.06
Envelope Rg envelope_rg22.64
Shape Rg shape_rg22.31
Total Rg total_rg23.32
Total atoms total_atoms2327
Residues n_residues296
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 dmax81.9
Rg (real space) rg_real23.37
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.7210e+07
I(0) uncertainty (real space) i0_real_error2.5780e+05
Rg (reciprocal space) rg_reciprocal23.34
I(0) (reciprocal space) i0_reciprocal17210000.0000
Solution quality estimate total_estimate0.8497
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.539
Kurtosis Kurtosis kurtosis-0.062
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6478000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.861; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1na8a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.10 — Clathrin adaptor appendage domain
Family Family familyb.1.10.2 — gamma-adaptin C-terminal appendage domain-like
Domain ID domain_idd1na8a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1na8b_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.10 — Clathrin adaptor appendage domain
Family Family familyb.1.10.2 — gamma-adaptin C-terminal appendage domain-like

CATH v4.4 (2 domains)

Domain ID domain_id1na8A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1230 — Gamma-adaptin ear (GAE) domain
Domain ID domain_id1na8B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1230 — Gamma-adaptin ear (GAE) domain

8. Citations (1)

9. Files and Curves (10)