6VZR: Engineered TTLL6
Engineered TTLL6 bound to the initiation analog. Determined by X-ray diffraction at 2.6 Å resolution. Released 12 Aug 2020.
- Method
- X-ray diffraction
- Resolution
- 2.6 Å
- Organism
- Mus musculus
- Chains
- 6
- Atoms
- 13,457
- Mol. weight
- 221.51 kDa
- Ligands
- 2TI, ADP, MG
- Released
- 12 Aug 2020
Explore 6VZR in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6VZR contains 78 α-helices and 80 β-strands across 6 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.
Chain A: 19 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 58-60 | 3 | |
| β-strand | 61-66 | 6 | 1 |
| α-helix | 70-79 | 10 | |
| β-strand | 82-83 | 2 | 1 |
| β-strand | 92-95 | 4 | 1 |
| α-helix | 101-104 | 4 | |
| β-strand | 112-113 | 2 | 1 |
| α-helix | 120-123 | 4 | |
| α-helix | 125-138 | 14 | |
| β-strand | 149-152 | 4 | 2 |
| α-helix | 156-165 | 10 | |
| β-strand | 171-174 | 4 | 2 |
| β-strand | 185-187 | 3 | 2 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-203 | 5 | 2 |
| β-strand | 208 | 1 | 3 |
| β-strand | 210-211 | 2 | 4 |
| β-strand | 214-215 | 2 | 4 |
| β-strand | 216-227 | 12 | 5 |
| β-strand | 230-235 | 6 | 5 |
| β-strand | 239-242 | 4 | 5 |
| α-helix | 243 | 1 | |
| α-helix | 258-261 | 4 | |
| α-helix | 265-268 | 4 | |
| β-strand | 283-285 | 3 | 5 |
| α-helix | 286-295 | 10 | |
| α-helix | 300-317 | 18 | |
| α-helix | 319-329 | 11 | |
| β-strand | 339 | 1 | 1 |
| β-strand | 341-349 | 9 | 5 |
| β-strand | 350 | 1 | 3 |
| α-helix | 354 | 1 | |
| β-strand | 355-361 | 7 | 5 |
| α-helix | 371-387 | 17 | |
| α-helix | 390-392 | 3 | |
| α-helix | 395-410 | 16 | |
| α-helix | 417-437 | 21 | |
| β-strand | 444-448 | 5 | 5 |
| α-helix | 453-459 | 7 | |
Chain B: 19 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 58-60 | 3 | |
| β-strand | 61-66 | 6 | 6 |
| α-helix | 70-79 | 10 | |
| β-strand | 82-83 | 2 | 6 |
| β-strand | 92-95 | 4 | 6 |
| α-helix | 101-104 | 4 | |
| β-strand | 112-113 | 2 | 6 |
| α-helix | 120-123 | 4 | |
| α-helix | 125-138 | 14 | |
| β-strand | 149-152 | 4 | 7 |
| α-helix | 156-165 | 10 | |
| β-strand | 171-174 | 4 | 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 | 210-211 | 2 | 9 |
| β-strand | 214-215 | 2 | 9 |
| β-strand | 216-227 | 12 | 10 |
| β-strand | 230-235 | 6 | 10 |
| β-strand | 239-242 | 4 | 10 |
| α-helix | 243 | 1 | |
| α-helix | 258-261 | 4 | |
| α-helix | 265-268 | 4 | |
| β-strand | 283-285 | 3 | 10 |
| α-helix | 286-295 | 10 | |
| α-helix | 300-317 | 18 | |
| α-helix | 319-329 | 11 | |
| β-strand | 339 | 1 | 6 |
| β-strand | 341-349 | 9 | 10 |
| β-strand | 350 | 1 | 8 |
| α-helix | 354 | 1 | |
| β-strand | 355-361 | 7 | 10 |
| α-helix | 371-387 | 17 | |
| α-helix | 390-392 | 3 | |
| α-helix | 395-410 | 16 | |
| α-helix | 415-437 | 23 | |
| β-strand | 444-448 | 5 | 10 |
| α-helix | 453-459 | 7 | |
Chain C: 19 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 58-60 | 3 | |
| β-strand | 61-66 | 6 | 11 |
| α-helix | 70-79 | 10 | |
| β-strand | 82-83 | 2 | 11 |
| β-strand | 92-95 | 4 | 11 |
| α-helix | 101-105 | 5 | |
| β-strand | 112-113 | 2 | 11 |
| α-helix | 120-123 | 4 | |
| α-helix | 125-138 | 14 | |
| β-strand | 149-152 | 4 | 12 |
| α-helix | 156-165 | 10 | |
| β-strand | 171-174 | 4 | 12 |
| β-strand | 185-187 | 3 | 12 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-203 | 5 | 12 |
| β-strand | 208 | 1 | 13 |
| β-strand | 210-211 | 2 | 14 |
| β-strand | 214-215 | 2 | 14 |
| β-strand | 216-227 | 12 | 15 |
| β-strand | 230-235 | 6 | 15 |
| β-strand | 239-242 | 4 | 15 |
| α-helix | 243 | 1 | |
| α-helix | 258-261 | 4 | |
| α-helix | 265-268 | 4 | |
| β-strand | 283-285 | 3 | 15 |
| α-helix | 286-295 | 10 | |
| α-helix | 300-317 | 18 | |
| α-helix | 319-329 | 11 | |
| β-strand | 339 | 1 | 11 |
| β-strand | 341-349 | 9 | 15 |
| β-strand | 350 | 1 | 13 |
| α-helix | 354 | 1 | |
| β-strand | 355-361 | 7 | 15 |
| α-helix | 371-387 | 17 | |
| α-helix | 390-392 | 3 | |
| α-helix | 395-410 | 16 | |
| α-helix | 415-440 | 26 | |
| β-strand | 444-448 | 5 | 15 |
| α-helix | 453-459 | 7 | |
Chain D: 19 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 58-60 | 3 | |
| β-strand | 61-66 | 6 | 16 |
| α-helix | 70-79 | 10 | |
| β-strand | 82-83 | 2 | 16 |
| β-strand | 92-95 | 4 | 16 |
| α-helix | 101-105 | 5 | |
| β-strand | 112-113 | 2 | 16 |
| α-helix | 120-123 | 4 | |
| α-helix | 125-138 | 14 | |
| β-strand | 149-152 | 4 | 17 |
| α-helix | 156-165 | 10 | |
| β-strand | 171-174 | 4 | 17 |
| β-strand | 185-187 | 3 | 17 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-203 | 5 | 17 |
| β-strand | 208 | 1 | 18 |
| β-strand | 210-211 | 2 | 19 |
| β-strand | 214-215 | 2 | 19 |
| β-strand | 216-227 | 12 | 20 |
| β-strand | 230-235 | 6 | 20 |
| β-strand | 239-242 | 4 | 20 |
| α-helix | 243 | 1 | |
| α-helix | 258-261 | 4 | |
| α-helix | 265-268 | 4 | |
| β-strand | 283-285 | 3 | 20 |
| α-helix | 286-295 | 10 | |
| α-helix | 300-317 | 18 | |
| α-helix | 319-329 | 11 | |
| β-strand | 339 | 1 | 16 |
| β-strand | 341-349 | 9 | 20 |
| β-strand | 350 | 1 | 18 |
| α-helix | 354 | 1 | |
| β-strand | 355-361 | 7 | 20 |
| α-helix | 371-387 | 17 | |
| α-helix | 390-392 | 3 | |
| α-helix | 395-410 | 16 | |
| α-helix | 415-437 | 23 | |
| β-strand | 444-448 | 5 | 20 |
| α-helix | 453-459 | 7 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-16 | 9 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-15 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Tubulin polyglutamylase TTLL6 | A, B, C, D | protein | 453 | Mus musculus | A4Q9E8 (AlphaFold model) |
| TTLL6 unregistered chain | F | protein | 12 | Mus musculus | |
| TTLL6 unregistered chain | G | protein | 11 | Mus musculus | |
Sequence of entity 1 (A, B, C, D), FASTA
>6VZR_1 Tubulin polyglutamylase TTLL6 (chains A, B, C, D)
GKKKRKKKRLVINLSNCRYDSVRRAAQQYGLREAGDNDDWTLYWTDYSVSLERVMEMKSY
QKINHFPGMSEICRKDLLARNMSRMLKLFPKDFHFFPRTWCLPADWGDLQTYSRTRKNKT
YICKPDSGARGRGIFITRSVKEIKPGEDMICQLYISKPFIIDGFKFDLRVYVLVTSCDPL
RVFVYNEGLARFATTSYSHPNLDNLDEICMHLTNYSINKHSSNFVQDAFSGSKRKLSTFN
SYMKTHGYDVEQIWRGIEDVIIKTLISAHPVIKHNYHTCFPSHTLNSACFEILGFDILLD
RKLKPWLLEVNISPSFSTDSKLDKEVKDSLLYDALVLINLGNCDKKKVLEEERQRGRFLQ
QCPNREIRLEEVKGFQAMRLQKTEEYEKKNCGGFRLIYPGLNLEKYDKFFQDNSSLFQNT
VASRARELYARQLIQELRQKQEKKVFLKKARKE
Sequence of entity 2 (F), FASTA
>6VZR_2 TTLL6 unregistered chain (chains F)
XXXXXXXXXXXX
Sequence of entity 3 (G), FASTA
>6VZR_3 TTLL6 unregistered chain (chains G)
XXXXXXXXXXX
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 2TI | (2~{S})-2-[[[(3~{R})-3-acetamido-4-(ethylamino)-4-oxidanylidene-butyl]-phosphon… | C14 H26 N2 O11 P2 | 4 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 4 |
| MG | Magnesium ion | Mg | 8 |
Water and common crystallization additives (GOL) are not listed.
Primary citation
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:
- 6VZU 1.98 Å, TTLL6 bound to alpha-elongation analog
- 6VZT 2.18 Å, TTLL6 bound to ATP
- 6VZV 2.33 Å, TTLL6 bound to gamma-elongation analog
- 6VZW 2.5 Å, TTLL6 bound to the initiation analog
- 6VZS 2.66 Å, Engineered TTLL6 mutant bound to gamma-elongation analog
- 6VZQ 3.08 Å, Engineered TTLL6 mutant bound to alpha-elongation analog
- 8T42 3.6 Å, Model of TTLL6 MTBH1-2 bound to microtubule
- 8U3Z 3.6 Å, Model of TTLL6 bound to microtubule from composite map
Browse structure collections
About this viewer
MolViewer shows 6VZR 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.