9b0b

Structure of Optineurin bound to HOIP NZF1 domain

Method: X-RAY DIFFRACTION Dmax: 127.1 Å Quality: REASONABLE

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 419–512 Chain B; UniProt 419–512 Fragment:Optineurin UBAN domain, residues 419-512 Mutation:C472S, S473E E3 ubiquitin-protein ligase RNF31 × 1 (Q96EP0) PGE TRIETHYLENE GLYCOL × 5 PG4 TETRAETHYLENE GLYCOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293 K;3:1 (protein:mother liquor: 10% PEG 8K, 20% ethylene glycol, 0.1 M Tris/Bicine pH 8.5, 0.03 M MgCl2 and 0.03 M CaCl2. cryoprotected in mother liquor containing 10% glycerol Resolution 1.70 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 419–512 Chain D; UniProt 419–512 Fragment:Optineurin UBAN domain, residues 419-512 Mutation:C472S, S473E E3 ubiquitin-protein ligase RNF31 × 1 (Q96EP0) PGE TRIETHYLENE GLYCOL × 5 PG4 TETRAETHYLENE GLYCOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293 K;3:1 (protein:mother liquor: 10% PEG 8K, 20% ethylene glycol, 0.1 M Tris/Bicine pH 8.5, 0.03 M MgCl2 and 0.03 M CaCl2. cryoprotected in mother liquor containing 10% glycerol Resolution 1.70 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OPTN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–96; UniProt 419–512 Author chain B; PDBConstruct 3–96; UniProt 419–512 Author chain C; PDBConstruct 3–96; UniProt 419–512 Author chain D; PDBConstruct 3–96; UniProt 419–512

E3 ubiquitin-protein ligase RNF31

Homo sapiens

UniProt Q96EP0

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 350–379 Not recorded Optineurin × 2 (Q96CV9) PGE TRIETHYLENE GLYCOL × 5 PG4 TETRAETHYLENE GLYCOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293 K;3:1 (protein:mother liquor: 10% PEG 8K, 20% ethylene glycol, 0.1 M Tris/Bicine pH 8.5, 0.03 M MgCl2 and 0.03 M CaCl2. cryoprotected in mother liquor containing 10% glycerol Resolution 1.70 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 350–379 Not recorded Optineurin × 2 (Q96CV9) PGE TRIETHYLENE GLYCOL × 5 PG4 TETRAETHYLENE GLYCOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293 K;3:1 (protein:mother liquor: 10% PEG 8K, 20% ethylene glycol, 0.1 M Tris/Bicine pH 8.5, 0.03 M MgCl2 and 0.03 M CaCl2. cryoprotected in mother liquor containing 10% glycerol Resolution 1.70 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.

35 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNF31_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–30; UniProt 350–379 Author chain G; PDBConstruct 1–30; UniProt 350–379

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 9b0b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b0b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b0b
Deposition date deposition_date2024-03-11
最后修订 last_revision2024-07-31
Structure title titleStructure of Optineurin bound to HOIP NZF1 domain
Keywords keywordsoptineurin, autophagy, mitophagy, xenophagy, UBAN, NZF, HOIP, LUBAC, linear Ub chain, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.46
Radius of gyration Rg (electron density) rg_electron37.74
Forward intensity I(0) i035462000.00
Molecular weight molecular_weight46252.0 kDa
Excluded volume excluded_volume57658 ų
Envelope volume envelope_volume83454 ų
Hydration-shell volume shell_volume21258 ų
Envelope diameter envelope_diameter134.6
Shell Rg shell_rg36.69
Envelope Rg envelope_rg38.35
Shape Rg shape_rg37.78
Total Rg total_rg37.52
Total atoms total_atoms3217
Residues n_residues395
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 dmax127.1
Rg (real space) rg_real36.84
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real3.5460e+07
I(0) uncertainty (real space) i0_real_error5.6610e+05
Rg (reciprocal space) rg_reciprocal36.61
I(0) (reciprocal space) i0_reciprocal35450000.0000
Solution quality estimate total_estimate0.5782
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary47.3
Skewness Skewness skewness0.404
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1255000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.693; Stabil: 1.000; Sysdev: 0.048; Positv: 1.000; Valcen: 0.510; Smooth: 0.781

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)