4gvd

Crystal Structure of T-cell Lymphoma Invasion and Metastasis-1 PDZ in complex with Syndecan1 Peptide

Method: X-RAY DIFFRACTION Dmax: 61.7 Å Quality: GOOD

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

T-lymphoma invasion and metastasis-inducing protein 1

Homo sapiens

UniProt Q13009

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 841–930 Fragment:PDZ domain (UNP residues 841-930) Syndecan-1 × 1 (P18827) CL CHLORIDE ION × 2 NA SODIUM ION × 1 ANS 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;291 K;0.1 M MES, 20% PEG8000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.85 Å R-free 0.243
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 841–930 Fragment:PDZ domain (UNP residues 841-930) Syndecan-1 × 1 (P18827) CL CHLORIDE ION × 1 NA SODIUM ION × 1 ANS 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;291 K;0.1 M MES, 20% PEG8000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.85 Å R-free 0.243

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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIAM1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–94; UniProt 841–930 Author chain B; PDBConstruct 5–94; UniProt 841–930

Syndecan-1

OrganismNot specified

UniProt P18827

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 D; UniProt 303–310 Fragment:UNP residues 303-310 T-lymphoma invasion and metastasis-inducing protein 1 × 1 (Q13009) CL CHLORIDE ION × 2 NA SODIUM ION × 1 ANS 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;291 K;0.1 M MES, 20% PEG8000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.85 Å R-free 0.243
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 303–310 Fragment:UNP residues 303-310 T-lymphoma invasion and metastasis-inducing protein 1 × 1 (Q13009) CL CHLORIDE ION × 1 NA SODIUM ION × 1 ANS 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;291 K;0.1 M MES, 20% PEG8000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.85 Å R-free 0.243

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SDC1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–8; UniProt 303–310 Author chain D; PDBConstruct 1–8; UniProt 303–310

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 4gvd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gvd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gvd
Deposition date deposition_date2012-08-30
Structure title titleCrystal Structure of T-cell Lymphoma Invasion and Metastasis-1 PDZ in complex with Syndecan1 Peptide
Keywords keywords;conformational change during phosphorylation, different binding pocket from phosphorylated sydencan1, scaffold signaling protein for cell adhesion and cell junction, sydencan1 N-terminal Thr dansylation, 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_guinier18.69
Radius of gyration Rg (electron density) rg_electron17.63
Forward intensity I(0) i08078660.00
Molecular weight molecular_weight20900.0 kDa
Excluded volume excluded_volume26176 ų
Envelope volume envelope_volume31480 ų
Hydration-shell volume shell_volume15396 ų
Envelope diameter envelope_diameter61.9
Shell Rg shell_rg23.01
Envelope Rg envelope_rg17.75
Shape Rg shape_rg17.61
Total Rg total_rg18.60
Total atoms total_atoms1465
Residues n_residues192
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 dmax61.7
Rg (real space) rg_real18.64
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real8.0790e+06
I(0) uncertainty (real space) i0_real_error9.2240e+04
Rg (reciprocal space) rg_reciprocal18.65
I(0) (reciprocal space) i0_reciprocal8079000.0000
Solution quality estimate total_estimate0.8864
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.1
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1474000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4gvdA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain
Domain ID domain_id4gvdB00
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)