3e2b

Crystal structure of Dynein Light chain LC8 in complex with a peptide derived from Swallow

Method: X-RAY DIFFRACTION Dmax: 43.6 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–89 Not recorded Protein swallow 16-residue peptide × 2 (P40688) ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;0.2M sodium potassium tartrate, 0.1M sodium citrate, 2.0M ammonium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.266

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 26 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

Protein swallow 16-residue peptide

OrganismNot specified

UniProt P40688

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 C; UniProt 281–296 Not recorded Dynein light chain 1, cytoplasmic × 2 (Q24117) ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;0.2M sodium potassium tartrate, 0.1M sodium citrate, 2.0M ammonium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.266

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 SWA_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–16; UniProt 281–296

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 3e2b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3e2b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3e2b
Deposition date deposition_date2008-08-05
Structure title titleCrystal structure of Dynein Light chain LC8 in complex with a peptide derived from Swallow
Keywords keywordsprotein-peptide complex, transport protein, Cytoplasm, Dynein, Microtubule, Motor protein; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.96
Radius of gyration Rg (electron density) rg_electron12.43
Forward intensity I(0) i02629060.00
Molecular weight molecular_weight11191.0 kDa
Excluded volume excluded_volume13992 ų
Envelope volume envelope_volume15180 ų
Hydration-shell volume shell_volume10397 ų
Envelope diameter envelope_diameter41.7
Shell Rg shell_rg18.24
Envelope Rg envelope_rg12.78
Shape Rg shape_rg12.40
Total Rg total_rg13.85
Total atoms total_atoms788
Residues n_residues97
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 dmax43.6
Rg (real space) rg_real13.86
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real2.6290e+06
I(0) uncertainty (real space) i0_real_error2.4350e+04
Rg (reciprocal space) rg_reciprocal13.86
I(0) (reciprocal space) i0_reciprocal2629000.0000
Solution quality estimate total_estimate0.8902
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.8
Skewness Skewness skewness0.086
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha537600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3e2ba_
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

CATH v4.4 (1 domains)

Domain ID domain_id3e2bA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology740 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase
Homologous superfamily homologous superfamily10 — Protein Inhibitor Of Neuronal Nitric Oxide Synthase;

8. Citations (2)

9. Files and Curves (10)