1v1t

Crystal structure of the PDZ tandem of human syntenin in complex with TNEYKV peptide

Method: X-RAY DIFFRACTION Dmax: 77.8 Å Quality: GOOD

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

SYNTENIN 1

HOMO SAPIENS

UniProt O00560

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 113–273 Chain B; UniProt 113–273 Fragment:PDZ TANDEM, RESIDUES 108-273 TNEYKV PEPTIDE × 2 BEZ BENZOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;20% PEG3350, 0.2M NH4CL, VAPOR DIFFUSION, SITTING DROP, pH 7.50 Resolution 1.80 Å R-free 0.229

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.

64 other PDB entries and 186 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SDB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–166; UniProt 113–273 Author chain B; PDBConstruct 6–166; UniProt 113–273

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 1v1t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1v1t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1v1t
Deposition date deposition_date2004-04-23
Structure title titleCrystal structure of the PDZ tandem of human syntenin in complex with TNEYKV peptide
Keywords keywordsCELL ADHESION, ADHESION-COMPLEX, PDZ DOMAIN, SCAFFOLDING PROTEIN; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.05
Radius of gyration Rg (electron density) rg_electron22.13
Forward intensity I(0) i023901200.00
Molecular weight molecular_weight36869.0 kDa
Excluded volume excluded_volume46161 ų
Envelope volume envelope_volume56635 ų
Hydration-shell volume shell_volume21632 ų
Envelope diameter envelope_diameter82.9
Shell Rg shell_rg28.41
Envelope Rg envelope_rg22.38
Shape Rg shape_rg22.12
Total Rg total_rg22.98
Total atoms total_atoms2585
Residues n_residues336
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 dmax77.8
Rg (real space) rg_real23.02
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real2.3900e+07
I(0) uncertainty (real space) i0_real_error3.2910e+05
Rg (reciprocal space) rg_reciprocal23.03
I(0) (reciprocal space) i0_reciprocal23900000.0000
Solution quality estimate total_estimate0.7985
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis-0.386
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19840000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1v1ta1
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_idd1v1ta2
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_idd1v1ta3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1v1tb1
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_idd1v1tb2
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_idd1v1tb3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id1v1tA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain
Domain ID domain_id1v1tA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain
Domain ID domain_id1v1tB01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain
Domain ID domain_id1v1tB02
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)