Complex between the dynein light chain DYNLL1/DLC8 and the specific domain of large myelin-associated glycoprotein L-MAG. Determined by X-ray diffraction at 1.98 Å resolution. Released 10 Oct 2018.
Explore 6GZJ in 3D Show helices and sheets RCSB PDB PDBe
6GZJ contains 3 α-helices and 6 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-5 | 2 | |
| β-strand | 6-13 | 8 | 1 |
| α-helix | 15-31 | 17 | |
| α-helix | 35-50 | 16 | |
| β-strand | 54-59 | 6 | 1 |
| β-strand | 63-69 | 7 | 2 |
| β-strand | 72-78 | 7 | 1 |
| β-strand | 81-87 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 607-613 | 7 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dynein light chain 1, cytoplasmic | A | protein | 90 | Homo sapiens | P63167 (AlphaFold model) |
| Myelin-associated glycoprotein | B | protein | 54 | Mus musculus | P20917 (AlphaFold model) |
>6GZJ_1 Dynein light chain 1, cytoplasmic (chains A) SMCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVG RNFGSYVTHETKHFIYFYLGQVAILLFKSG
>6GZJ_2 Myelin-associated glycoprotein (chains B) SEKRLGSERRLLGLRGESPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK
High-affinity heterotetramer formation between the large myelin-associated glycoprotein and the dynein light chain DYNLL1. Myllykoski, M., Eichel, M.A., Jung, R.B. et al. J Neurochem (2018) 147:764-783. DOI 10.1111/jnc.14598 · PubMed
Other PDB entries of the same protein (UniProt P63167 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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