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6irr

Solution structure of DISC1/ATF4 complex

Method: SOLUTION NMR Dmax: 54.5 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Disrupted in schizophrenia 1 homolog,Cyclic AMP-dependent transcription factor ATF-4

Mus musculus

UniProt Q06507

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 314–349 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；303 K；Ionic strength (raw mmCIF value) 100mM potassium phosphate；Pressure ambient NMR sample composition：0.8 mM [U-100% 13C; U-100% 15N] DISC1/ATF4 complex, 1 mM DTT, 1 mM EDTA, 100 mM potassium phosphate, 100% D2O | 100% D2O NMR sample composition：0.8 mM [U-99% 15N] DISC1/ATF4 complex, 1 mM DTT, 1 mM EDTA, 100 mM potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：0.8 mM DISC1/ATF4 complex, 1 mM DTT, 1 mM EDTA, 100 mM potassium phosphate, 100% D2O | 100% D2O Resolution not provided

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name ATF4_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 98–133； UniProt 314–349

Disrupted in schizophrenia 1 homolog,Cyclic AMP-dependent transcription factor ATF-4

Mus musculus

UniProt Q811T9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 763–850 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；303 K；Ionic strength (raw mmCIF value) 100mM potassium phosphate；Pressure ambient NMR sample composition：0.8 mM [U-100% 13C; U-100% 15N] DISC1/ATF4 complex, 1 mM DTT, 1 mM EDTA, 100 mM potassium phosphate, 100% D2O | 100% D2O NMR sample composition：0.8 mM [U-99% 15N] DISC1/ATF4 complex, 1 mM DTT, 1 mM EDTA, 100 mM potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：0.8 mM DISC1/ATF4 complex, 1 mM DTT, 1 mM EDTA, 100 mM potassium phosphate, 100% D2O | 100% D2O Resolution not provided

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.

Other PDB Difference from Current Entry 6IRR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5YI4 Solution Structure of the DISC1/Ndel1 complex Deposited 2017-10-02 Different construct Different experimental conditions Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 765–852（88 aa） Fragment：UNP residues 765-852,UNP residues 238-284
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 50 NaCl；Pressure 1
NMR sample composition 0.8 mM [U-99% 13C; U-99% 15N] DISC1_Ndel1, 100% D2O | 100% D2O
NMR sample composition 0.8 mM [U-99% 15N] DISC1_Ndel1, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.8 mM [U-99% 13C; U-99% 15N] DISC1_Ndel1, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.8 mM no labelling DISC1_Ndel1, 100% D2O | 100% D2O
Resolution not provided
9RUX Cryo-EM structure of DISC1 core Deposited 2025-07-05 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 322–722（401 aa）
Chain B 322–722（401 aa）
Chain C 322–722（401 aa）
Chain D 322–722（401 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DISC1_MOUSE
Isoform Q811T9-2
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–88； UniProt 763–850

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 6irr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6irr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6irr
Deposition date deposition_date2018-11-14
Structure title titleSolution structure of DISC1/ATF4 complex
Keywords keywordsScaffold protein, Psychiatric disorder, coiled coil, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier21.19 Å
Radius of gyration Rg (electron density) rg_electron20.66 Å
Forward intensity I(0) i01205660000.00
Molecular weight molecular_weight290810.0 kDa
Excluded volume excluded_volume364220 ų
Envelope volume envelope_volume109120 ų
Hydration-shell volume shell_volume33198 ų
Envelope diameter envelope_diameter93.0 Å
Shell Rg shell_rg35.02 Å
Envelope Rg envelope_rg27.24 Å
Shape Rg shape_rg20.71 Å
Total Rg total_rg20.94 Å
Total atoms total_atoms41160
Residues n_residues2660
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax54.5 Å
Rg (real space) rg_real19.97 Å
Rg uncertainty (real space) rg_real_error0.09 Å
I(0) (real space) i0_real1.1460e+09
I(0) uncertainty (real space) i0_real_error1.1090e+07
Rg (reciprocal space) rg_reciprocal21.29 Å
I(0) (reciprocal space) i0_reciprocal1206000000.0000
Solution quality estimate total_estimate0.6833
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary20.0 Å
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.635
Angular range angular_range— – 0.3750 Å−1
Current regularization parameter α current_alpha2.9180
Highest regularization parameter α highest_alpha858400.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.982; Stabil: 0.980; Sysdev: 0.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)