3p8m

X-ray diffraction
2.9Å resolution

Human dynein light chain (DYNLL2) in complex with an in vitro evolved peptide dimerized by leucine zipper

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-136529 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dynein light chain 2, cytoplasmic Chains: A, B
Molecule details ›
Chains: A, B
Length: 92 amino acids
Theoretical weight: 10.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96FJ2 (Residues: 1-89; Coverage: 100%)
Gene names: DLC2, DYNLL2
Sequence domains: Dynein light chain type 1
Structure domains: Protein Inhibitor Of Neuronal Nitric Oxide Synthase;
General control transcription factor GCN4 Chains: C, D
Molecule details ›
Chains: C, D
Length: 46 amino acids
Theoretical weight: 5.11 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P03069 (Residues: 238-245, 250-281; Coverage: 14%)
Gene names: AAS101, AAS3, ARG9, GCN4, YEL009C
Sequence domains: Basic region leucine zipper
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 53.839Å b: 68.415Å c: 101.677Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.248 0.295
Expression system: Escherichia coli