7czm

Crystal structure of FIP200 Claw/p-OPtineurin LIR complex

Method: X-RAY DIFFRACTION Dmax: 72.4 Å Quality: GOOD

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

RB1-inducible coiled-coil protein 1

Homo sapiens

UniProt Q8TDY2

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 1490–1594 Chain B; UniProt 1490–1594 Not recorded Optineurin LIR × 2 (Q96CV9) GOL GLYCEROL × 2 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;Potassium iodide, MES pH 6.5, PEG 4000 Resolution 2.00 Å R-free 0.223

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.

17 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBCC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–108; UniProt 1490–1594 Author chain B; PDBConstruct 4–108; UniProt 1490–1594

Optineurin LIR

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 C; UniProt 173–185 Chain D; UniProt 173–185 Non-standard monomer:Yes (specific site not provided by mmCIF) RB1-inducible coiled-coil protein 1 × 2 (Q8TDY2) GOL GLYCEROL × 2 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;Potassium iodide, MES pH 6.5, PEG 4000 Resolution 2.00 Å R-free 0.223

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 C; PDBConstruct 1–13; UniProt 173–185 Author chain D; PDBConstruct 1–13; UniProt 173–185

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 7czm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7czm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7czm
Deposition date deposition_date2020-09-09
Structure title titleCrystal structure of FIP200 Claw/p-OPtineurin LIR complex
Keywords keywordsautophagy, FIP200, Optineurin, SIGNALING PROTEIN, SIGNALING PROTEIN-PROTEIN BINDING complex; SIGNALING PROTEIN/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.63
Radius of gyration Rg (electron density) rg_electron20.34
Forward intensity I(0) i010384500.00
Molecular weight molecular_weight24687.0 kDa
Excluded volume excluded_volume31259 ų
Envelope volume envelope_volume38312 ų
Hydration-shell volume shell_volume16855 ų
Envelope diameter envelope_diameter72.7
Shell Rg shell_rg25.49
Envelope Rg envelope_rg20.55
Shape Rg shape_rg20.24
Total Rg total_rg21.45
Total atoms total_atoms1734
Residues n_residues204
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 dmax72.4
Rg (real space) rg_real21.75
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real1.0380e+07
I(0) uncertainty (real space) i0_real_error1.6670e+05
Rg (reciprocal space) rg_reciprocal21.73
I(0) (reciprocal space) i0_reciprocal10380000.0000
Solution quality estimate total_estimate0.7970
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis-0.283
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2418000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.849; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)