1vj6

PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein

Method: SOLUTION NMR Dmax: 39.5 Å Quality: GOOD

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

protein-tyrosine-phosphatase (nonreceptor type 13)

Mus musculus

UniProt Q64512

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1350–1443 Fragment:PDZ2 domain Adenomatous polyposis coli protein × 1 (Q61315) SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 100;Pressure 1 NMR sample composition:1mM PDZ2 protein, U-15N,13C; 3mM APC peptide, unlabelled | 50 mM KH2PO4/K2HPO4 50 mM KCl, pH 6.8, H2O/D2O (95%/5%) 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTN13_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–102; UniProt 1350–1443

Adenomatous polyposis coli protein

OrganismNot specified

UniProt Q61315

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2834–2845 Fragment:C-terminus of APC protein-tyrosine-phosphatase (nonreceptor type 13) × 1 (Q64512) SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 100;Pressure 1 NMR sample composition:1mM PDZ2 protein, U-15N,13C; 3mM APC peptide, unlabelled | 50 mM KH2PO4/K2HPO4 50 mM KCl, pH 6.8, H2O/D2O (95%/5%) 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APC_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–12; UniProt 2834–2845

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 1vj6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1vj6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1vj6
Deposition date deposition_date2004-02-03
Structure title titlePDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein
Keywords keywordsPDZ, complex, APC, protein-protein interaction, PTP-BL, C-terminus, Hydrolase-Signaling Protein COMPLEX; Hydrolase/Signaling Protein
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.87
Radius of gyration Rg (electron density) rg_electron12.58
Forward intensity I(0) i01888620000.00
Molecular weight molecular_weight369780.0 kDa
Excluded volume excluded_volume464110 ų
Envelope volume envelope_volume25133 ų
Hydration-shell volume shell_volume14153 ų
Envelope diameter envelope_diameter47.6
Shell Rg shell_rg20.92
Envelope Rg envelope_rg15.18
Shape Rg shape_rg12.56
Total Rg total_rg12.77
Total atoms total_atoms52815
Residues n_residues3535
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 dmax39.5
Rg (real space) rg_real12.77
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.8890e+09
I(0) uncertainty (real space) i0_real_error1.9650e+07
Rg (reciprocal space) rg_reciprocal12.77
I(0) (reciprocal space) i0_reciprocal1889000000.0000
Solution quality estimate total_estimate0.8121
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.0
Skewness Skewness skewness0.013
Kurtosis Kurtosis kurtosis-0.356
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha202400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.000

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_idd1vj6a1
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_idd1vj6a2
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_id1vj6A00
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)