5het

The third PDZ domain from the synaptic protein PSD-95 (G330T mutant)

Method: X-RAY DIFFRACTION Dmax: 57.1 Å Quality: GOOD

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

Disks large homolog 4

Rattus norvegicus

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 302–402 Fragment:PDZ-3 domain (UNP residues 302-402) Mutation:G330T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;Reservoir solution contained 1.05 M sodium citrate, pH 7.0. Equal amounts (1.5 microliters) of protein (7 mg/mL) and reservoir solution were mixed and equillibrated against 500 microliters of crystallization buffer. Resolution 2.00 Å R-free 0.213

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 6–106; UniProt 302–402

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 5het

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5het
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5het
Deposition date deposition_date2016-01-06
Structure title titleThe third PDZ domain from the synaptic protein PSD-95 (G330T mutant)
Keywords keywordsPDZ, GLGF, DHR, adhesion, synapse, synaptic density, peptide-binding domain, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.87
Radius of gyration Rg (electron density) rg_electron14.51
Forward intensity I(0) i03495380.00
Molecular weight molecular_weight12705.0 kDa
Excluded volume excluded_volume15726 ų
Envelope volume envelope_volume18719 ų
Hydration-shell volume shell_volume11369 ų
Envelope diameter envelope_diameter55.8
Shell Rg shell_rg19.87
Envelope Rg envelope_rg15.05
Shape Rg shape_rg14.50
Total Rg total_rg15.65
Total atoms total_atoms1775
Residues n_residues118
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 dmax57.1
Rg (real space) rg_real15.84
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real3.4950e+06
I(0) uncertainty (real space) i0_real_error4.2160e+04
Rg (reciprocal space) rg_reciprocal15.84
I(0) (reciprocal space) i0_reciprocal3495000.0000
Solution quality estimate total_estimate0.8459
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.5
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.131
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha515600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.940; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5heta1
Class classb — All beta proteins
Fold Fold foldb.36 — PDZ domain-like
Superfamily Superfamily superfamilyb.36.1 — PDZ domain-like
Family Family familyb.36.1.1 — PDZ domain
Domain ID domain_idd5heta2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5heta3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id5hetA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain

8. Citations (1)

9. Files and Curves (10)