9m0o

Crystal structure of OPTN 138-170 in complex with GTP-bound RAB8A1-176 (Q67L)

Method: X-RAY DIFFRACTION Dmax: 59.9 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ras-related protein Rab-8A

Homo sapiens

UniProt P61006

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–176 Mutation:Q67L Optineurin × 2 (Q96CV9) MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GOL GLYCEROL × 6 ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.05 M Imidazole pH 6.5, 0.5 M Sodium acetate trihydrate Resolution 1.83 Å R-free 0.222

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 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAB8A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–176; UniProt 1–176

Optineurin

Homo sapiens

UniProt Q96CV9

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 138–170 Not recorded Ras-related protein Rab-8A × 2 (P61006) MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GOL GLYCEROL × 6 ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.05 M Imidazole pH 6.5, 0.5 M Sodium acetate trihydrate Resolution 1.83 Å R-free 0.222

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.

13 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OPTN_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 4–36; UniProt 138–170

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 9m0o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m0o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m0o
Deposition date deposition_date2025-02-25
最后修订 last_revision2025-10-15
Structure title titleCrystal structure of OPTN 138-170 in complex with GTP-bound RAB8A1-176 (Q67L)
Keywords keywordsMembrane Trafficking, autophagy, small GTPase, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.75
Radius of gyration Rg (electron density) rg_electron17.64
Forward intensity I(0) i011696900.00
Molecular weight molecular_weight25264.0 kDa
Excluded volume excluded_volume31611 ų
Envelope volume envelope_volume37094 ų
Hydration-shell volume shell_volume17663 ų
Envelope diameter envelope_diameter60.5
Shell Rg shell_rg23.86
Envelope Rg envelope_rg18.18
Shape Rg shape_rg17.64
Total Rg total_rg18.61
Total atoms total_atoms1770
Residues n_residues213
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 dmax59.9
Rg (real space) rg_real18.67
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real1.1700e+07
I(0) uncertainty (real space) i0_real_error1.4140e+05
Rg (reciprocal space) rg_reciprocal18.68
I(0) (reciprocal space) i0_reciprocal11700000.0000
Solution quality estimate total_estimate0.7077
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1484000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 0.197; Positv: 1.000; Valcen: 0.997; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)