TTLL6 bound to ATP. Determined by X-ray diffraction at 2.18 Å resolution. Released 12 Aug 2020.
Explore 6VZT in 3D Show helices and sheets RCSB PDB PDBe
6VZT contains 34 α-helices and 40 β-strands across 3 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 | 58-60 | 3 | |
| β-strand | 61-63 | 3 | 1 |
| α-helix | 70-79 | 10 | |
| β-strand | 82-83 | 2 | 1 |
| β-strand | 92-93 | 2 | 1 |
| α-helix | 98-100 | 3 | |
| α-helix | 101-105 | 5 | |
| β-strand | 112-113 | 2 | 1 |
| α-helix | 120-123 | 4 | |
| α-helix | 125-138 | 14 | |
| β-strand | 149-152 | 4 | 2 |
| α-helix | 156-163 | 8 | |
| β-strand | 171-175 | 5 | 2 |
| β-strand | 185-187 | 3 | 2 |
| β-strand | 199-203 | 5 | 2 |
| β-strand | 208 | 1 | 3 |
| β-strand | 211 | 1 | 4 |
| β-strand | 214 | 1 | 4 |
| β-strand | 216-227 | 12 | 5 |
| β-strand | 230-235 | 6 | 5 |
| β-strand | 239-242 | 4 | 5 |
| α-helix | 258-261 | 4 | |
| α-helix | 265-268 | 4 | |
| β-strand | 283-285 | 3 | 5 |
| α-helix | 286-295 | 10 | |
| α-helix | 300-329 | 30 | |
| β-strand | 339 | 1 | 1 |
| β-strand | 341-349 | 9 | 5 |
| β-strand | 350 | 1 | 3 |
| β-strand | 355-361 | 7 | 5 |
| α-helix | 371-387 | 17 | |
| α-helix | 390-393 | 4 | |
| α-helix | 395-411 | 17 | |
| α-helix | 416-439 | 24 | |
| β-strand | 444-448 | 5 | 5 |
| α-helix | 453-459 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 58-60 | 3 | |
| β-strand | 61-63 | 3 | 6 |
| α-helix | 70-79 | 10 | |
| β-strand | 82-83 | 2 | 6 |
| β-strand | 92-93 | 2 | 6 |
| α-helix | 98-100 | 3 | |
| α-helix | 101-105 | 5 | |
| β-strand | 112-113 | 2 | 6 |
| α-helix | 120-123 | 4 | |
| α-helix | 125-138 | 14 | |
| β-strand | 149-152 | 4 | 7 |
| α-helix | 156-163 | 8 | |
| β-strand | 171-175 | 5 | 7 |
| β-strand | 185-187 | 3 | 7 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-203 | 5 | 7 |
| β-strand | 208 | 1 | 8 |
| β-strand | 211 | 1 | 9 |
| β-strand | 214 | 1 | 9 |
| β-strand | 216-227 | 12 | 10 |
| β-strand | 230-235 | 6 | 10 |
| β-strand | 239-242 | 4 | 10 |
| α-helix | 258-261 | 4 | |
| α-helix | 265-268 | 4 | |
| β-strand | 283-285 | 3 | 10 |
| α-helix | 286-295 | 10 | |
| α-helix | 300-329 | 30 | |
| β-strand | 339 | 1 | 6 |
| β-strand | 341-349 | 9 | 10 |
| β-strand | 350 | 1 | 8 |
| β-strand | 355-361 | 7 | 10 |
| α-helix | 371-387 | 17 | |
| α-helix | 390-393 | 4 | |
| α-helix | 395-408 | 14 | |
| α-helix | 418-439 | 22 | |
| β-strand | 444-448 | 5 | 10 |
| α-helix | 453-459 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-16 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin polyglutamylase TTLL6 | A, B | protein | 453 | Mus musculus | A4Q9E8 (AlphaFold model) |
| TTLL6 unregistered chain | D | protein | 11 | Mus musculus |
>6VZT_1 Tubulin polyglutamylase TTLL6 (chains A, B) GKKKRKKKRLVINLSNCRYDSVRRAAQQYGLREAGDNDDWTLYWTDYSVSLERVMEMKSY QKINHFPGMSEICRKDLLARNMSRMLKLFPKDFHFFPRTWCLPADWGDLQTYSRTRKNKT YICKPDSGCQGRGIFITRSVKEIKPGEDMICQLYISKPFIIDGFKFDLRVYVLVTSCDPL RVFVYNEGLARFATTSYSHPNLDNLDEICMHLTNYSINKHSSNFVQDAFSGSKRKLSTFN SYMKTHGYDVEQIWRGIEDVIIKTLISAHPVIKHNYHTCFPSHTLNSACFEILGFDILLD RKLKPWLLEVNHSPSFSTDSKLDKEVKDSLLYDALVLINLGNCDKKKVLEEERQRGRFLQ QCPNREIRLEEVKGFQAMRLQKTEEYEKKNCGGFRLIYPGLNLEKYDKFFQDNSSLFQNT VASRARELYARQLIQELRQKQEKKVFLKKARKE
>6VZT_2 TTLL6 unregistered chain (chains D) XXXXXXXXXXX
Water and common crystallization additives (GOL, SO4) are not listed.
Structural basis for polyglutamate chain initiation and elongation by TTLL family enzymes. Mahalingan, K.K., Keith Keenan, E., Strickland, M. et al. Nat Struct Mol Biol (2020) 27:802-813. DOI 10.1038/s41594-020-0462-0 · PubMed
Other PDB entries of the same protein (UniProt A4Q9E8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6VZT directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.