7k3j

Crystal structure of dLC8 in complex with Panoramix TQT+TQ peptide

Method: X-RAY DIFFRACTION Dmax: 102.2 Å Quality: GOOD

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

Dynein light chain 1, cytoplasmic

Drosophila melanogaster

UniProt Q24117

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–89 Chain G; UniProt 1–89 Chain I; UniProt 1–89 Chain K; UniProt 1–89 Not recorded Protein panoramix × 2 (Q9W2H9) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.2 M Li2SO4, 0.1 M Tris pH 8.5, 40% (v/v) PEG 400 Resolution 2.50 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–89 Chain E; UniProt 1–89 Not recorded Protein panoramix × 2 (Q9W2H9) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.2 M Li2SO4, 0.1 M Tris pH 8.5, 40% (v/v) PEG 400 Resolution 2.50 Å R-free 0.272

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.

17 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DYL1_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–89; UniProt 1–89 Author chain C; PDBConstruct 1–89; UniProt 1–89 Author chain E; PDBConstruct 1–89; UniProt 1–89 Author chain G; PDBConstruct 1–89; UniProt 1–89 Author chain I; PDBConstruct 1–89; UniProt 1–89 Author chain K; PDBConstruct 1–89; UniProt 1–89

Protein panoramix

Drosophila melanogaster

UniProt Q9W2H9

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 455–480 Chain H; UniProt 455–480 Fragment:residues 455-480 Dynein light chain 1, cytoplasmic × 4 (Q24117) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.2 M Li2SO4, 0.1 M Tris pH 8.5, 40% (v/v) PEG 400 Resolution 2.50 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 455–480 Chain F; UniProt 455–480 Fragment:residues 455-480 Dynein light chain 1, cytoplasmic × 2 (Q24117) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.2 M Li2SO4, 0.1 M Tris pH 8.5, 40% (v/v) PEG 400 Resolution 2.50 Å R-free 0.272

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.

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

View Construct and Data Evidence
UniProt name PANX_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–27; UniProt 455–480 Author chain D; PDBConstruct 2–27; UniProt 455–480 Author chain F; PDBConstruct 2–27; UniProt 455–480 Author chain H; PDBConstruct 2–27; UniProt 455–480

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 7k3j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7k3j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7k3j
Deposition date deposition_date2020-09-11
Structure title titleCrystal structure of dLC8 in complex with Panoramix TQT+TQ peptide
Keywords keywordsPiwi, transposon silencing, heterochromatin formation, piRNA pathway, transcriptional silencing, RNA BINDING PROTEIN, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.45
Radius of gyration Rg (electron density) rg_electron31.04
Forward intensity I(0) i066719400.00
Molecular weight molecular_weight64150.0 kDa
Excluded volume excluded_volume80006 ų
Envelope volume envelope_volume103330 ų
Hydration-shell volume shell_volume29781 ų
Envelope diameter envelope_diameter106.3
Shell Rg shell_rg35.94
Envelope Rg envelope_rg30.88
Shape Rg shape_rg31.04
Total Rg total_rg31.47
Total atoms total_atoms4519
Residues n_residues581
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 dmax102.2
Rg (real space) rg_real31.65
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real6.6720e+07
I(0) uncertainty (real space) i0_real_error9.6570e+05
Rg (reciprocal space) rg_reciprocal31.57
I(0) (reciprocal space) i0_reciprocal66710000.0000
Solution quality estimate total_estimate0.8766
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.418
Kurtosis Kurtosis kurtosis-0.536
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14120000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.879; Smooth: 0.851

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd7k3ja_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.39 — DLC
Superfamily Superfamily superfamilyd.39.1 — DLC
Family Family familyd.39.1.1 — DLC
Domain ID domain_idd7k3jc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.39 — DLC
Superfamily Superfamily superfamilyd.39.1 — DLC
Family Family familyd.39.1.1 — DLC
Domain ID domain_idd7k3je_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.39 — DLC
Superfamily Superfamily superfamilyd.39.1 — DLC
Family Family familyd.39.1.1 — DLC
Domain ID domain_idd7k3jg_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.39 — DLC
Superfamily Superfamily superfamilyd.39.1 — DLC
Family Family familyd.39.1.1 — DLC
Domain ID domain_idd7k3ji_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.39 — DLC
Superfamily Superfamily superfamilyd.39.1 — DLC
Family Family familyd.39.1.1 — DLC
Domain ID domain_idd7k3jk_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.39 — DLC
Superfamily Superfamily superfamilyd.39.1 — DLC
Family Family familyd.39.1.1 — DLC

8. Citations (1)

9. Files and Curves (10)