1oxz

Crystal Structure of the Human GGA1 GAT domain

Method: X-RAY DIFFRACTION Dmax: 64.1 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 141–326 Fragment:GAT domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;lithium sulfate, MES, ethylene glycol , pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.285

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 1–186; UniProt 141–326

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 1oxz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1oxz
Deposition date deposition_date2003-04-03
Structure title titleCrystal Structure of the Human GGA1 GAT domain
Keywords keywordsGGA1, GAT domain, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.11
Radius of gyration Rg (electron density) rg_electron23.40
Forward intensity I(0) i04801240.00
Molecular weight molecular_weight15083.0 kDa
Excluded volume excluded_volume18573 ų
Envelope volume envelope_volume24812 ų
Hydration-shell volume shell_volume11158 ų
Envelope diameter envelope_diameter86.3
Shell Rg shell_rg25.29
Envelope Rg envelope_rg23.88
Shape Rg shape_rg23.41
Total Rg total_rg23.67
Total atoms total_atoms1051
Residues n_residues132
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 dmax64.1
Rg (real space) rg_real21.38
Rg uncertainty (real space) rg_real_error0.19
I(0) (real space) i0_real4.5900e+06
I(0) uncertainty (real space) i0_real_error5.1980e+04
Rg (reciprocal space) rg_reciprocal23.58
I(0) (reciprocal space) i0_reciprocal4801000.0000
Solution quality estimate total_estimate0.6108
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.8
Skewness Skewness skewness0.519
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha1.7270
Highest regularization parameter α highest_alpha526600.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 0.989; Sysdev: 0.000; Positv: 1.000; Valcen: 0.581; Smooth: 0.000

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_idd1oxza_
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_id1oxzA01
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_id1oxzA02
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)