7cqf

Crystal structure of PSD-95 PDZ3 fused with ADAM22 C-terminal peptide

Method: X-RAY DIFFRACTION Dmax: 52.8 Å Quality: GOOD

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

Disks large homolog 4,Disintegrin and metalloproteinase domain-containing protein 22

Homo sapiens

UniProt P31016

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 309–422 Not recorded CL CHLORIDE ION × 1 CHT CHOLINE ION × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.2 M choline chloride, 0.1 M Tris-HCl (pH 7.5), 14 % (w/v) PEG 2000 MME Resolution 1.80 Å R-free 0.205

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.

40 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DLG4_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 18–131; UniProt 309–422

Disks large homolog 4,Disintegrin and metalloproteinase domain-containing protein 22

Homo sapiens

UniProt Q9P0K1

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 892–906 Not recorded CL CHLORIDE ION × 1 CHT CHOLINE ION × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.2 M choline chloride, 0.1 M Tris-HCl (pH 7.5), 14 % (w/v) PEG 2000 MME Resolution 1.80 Å R-free 0.205

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.

9 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADA22_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 136–150; UniProt 892–906

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 7cqf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7cqf
Deposition date deposition_date2020-08-10
Structure title titleCrystal structure of PSD-95 PDZ3 fused with ADAM22 C-terminal peptide
Keywords keywordsScaffold protein, Membrane receptor, 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_guinier15.35
Radius of gyration Rg (electron density) rg_electron13.98
Forward intensity I(0) i03467690.00
Molecular weight molecular_weight12793.0 kDa
Excluded volume excluded_volume15944 ų
Envelope volume envelope_volume18373 ų
Hydration-shell volume shell_volume11468 ų
Envelope diameter envelope_diameter51.1
Shell Rg shell_rg19.41
Envelope Rg envelope_rg14.48
Shape Rg shape_rg13.96
Total Rg total_rg15.19
Total atoms total_atoms901
Residues n_residues113
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 dmax52.8
Rg (real space) rg_real15.30
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real3.4680e+06
I(0) uncertainty (real space) i0_real_error4.4600e+04
Rg (reciprocal space) rg_reciprocal15.31
I(0) (reciprocal space) i0_reciprocal3468000.0000
Solution quality estimate total_estimate0.8557
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.030
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha628900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.720; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)