3wp0

Crystal structure of Dlg GK in complex with a phosphor-Lgl2 peptide

Method: X-RAY DIFFRACTION Dmax: 59.9 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 531–713 Fragment:UNP residues 533-713 Lethal(2) giant larvae protein homolog 2 × 1 (Q6P1M3) GOL GLYCEROL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;291 K;0.2M lithium chloride, 20% PEG3350, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.04 Å R-free 0.202

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 5–187; UniProt 531–713

Lethal(2) giant larvae protein homolog 2

OrganismNot specified

UniProt Q6P1M3

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 640–654 Fragment:UNP residues 640-654 Non-standard monomer:Yes (specific site not provided by mmCIF) Disks large homolog 4 × 1 (P31016) GOL GLYCEROL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;291 K;0.2M lithium chloride, 20% PEG3350, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.04 Å R-free 0.202

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.

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name L2GL2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 640–654

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 3wp0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3wp0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3wp0
Deposition date deposition_date2014-01-08
Structure title titleCrystal structure of Dlg GK in complex with a phosphor-Lgl2 peptide
Keywords keywordsMaGuk, Phosphorylation, Cell polarity, tumor suppressors, phosphorylation dependent, 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_guinier18.56
Radius of gyration Rg (electron density) rg_electron17.39
Forward intensity I(0) i09992080.00
Molecular weight molecular_weight22834.0 kDa
Excluded volume excluded_volume28394 ų
Envelope volume envelope_volume34265 ų
Hydration-shell volume shell_volume16707 ų
Envelope diameter envelope_diameter57.6
Shell Rg shell_rg23.11
Envelope Rg envelope_rg17.45
Shape Rg shape_rg17.40
Total Rg total_rg18.29
Total atoms total_atoms1606
Residues n_residues195
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 dmax59.9
Rg (real space) rg_real18.46
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real9.9920e+06
I(0) uncertainty (real space) i0_real_error1.3380e+05
Rg (reciprocal space) rg_reciprocal18.47
I(0) (reciprocal space) i0_reciprocal9992000.0000
Solution quality estimate total_estimate0.8196
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.136
Kurtosis Kurtosis kurtosis-0.507
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2097000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3wp0A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)