1tq3

Higher resolution crystal structure of the third PDZ domain of post synaptic PSD-95 protein

Method: X-RAY DIFFRACTION Dmax: 46.2 Å Quality: EXCELLENT

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

Presynaptic density protein 95

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:third PDZ domain (residues 302-402) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;295 K;1.0 M sodium citrate, 0.1 M HEPES, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.89 Å R-free 0.296

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 1tq3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1tq3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1tq3
Deposition date deposition_date2004-06-16
Structure title titleHigher resolution crystal structure of the third PDZ domain of post synaptic PSD-95 protein
Keywords keywordsPEPTIDE 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_guinier14.91
Radius of gyration Rg (electron density) rg_electron13.39
Forward intensity I(0) i03028030.00
Molecular weight molecular_weight11714.0 kDa
Excluded volume excluded_volume14526 ų
Envelope volume envelope_volume16590 ų
Hydration-shell volume shell_volume10790 ų
Envelope diameter envelope_diameter44.6
Shell Rg shell_rg18.75
Envelope Rg envelope_rg13.66
Shape Rg shape_rg13.37
Total Rg total_rg14.62
Total atoms total_atoms827
Residues n_residues110
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 dmax46.2
Rg (real space) rg_real14.82
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real3.0280e+06
I(0) uncertainty (real space) i0_real_error3.0320e+04
Rg (reciprocal space) rg_reciprocal14.82
I(0) (reciprocal space) i0_reciprocal3028000.0000
Solution quality estimate total_estimate0.9025
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.7
Skewness Skewness skewness0.135
Kurtosis Kurtosis kurtosis-0.417
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha422600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1tq3a2
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_idd1tq3a3
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_id1tq3A00
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)