Structural basis of tubulin detyrosination. Determined by X-ray diffraction at 2.2 Å resolution. Released 17 Jul 2019.
Explore 6JZC in 3D Show helices and sheets RCSB PDB PDBe
6JZC contains 31 α-helices and 20 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 50-51 | 2 | 1 |
| α-helix | 58-59 | 2 | |
| α-helix | 60-73 | 14 | |
| α-helix | 77-84 | 8 | |
| α-helix | 90-94 | 5 | |
| α-helix | 96-99 | 4 | |
| α-helix | 107-121 | 15 | |
| β-strand | 123 | 1 | 2 |
| β-strand | 128-129 | 2 | 1 |
| α-helix | 139-152 | 14 | |
| β-strand | 156 | 1 | 2 |
| α-helix | 158-169 | 12 | |
| β-strand | 176-186 | 11 | 3 |
| β-strand | 189-200 | 12 | 3 |
| β-strand | 203-207 | 5 | 3 |
| α-helix | 213-215 | 3 | |
| β-strand | 218-222 | 5 | 3 |
| α-helix | 225-237 | 13 | |
| α-helix | 241 | 1 | |
| β-strand | 242-248 | 7 | 3 |
| α-helix | 250-253 | 4 | |
| β-strand | 267-269 | 3 | 3 |
| α-helix | 271-273 | 3 | |
| α-helix | 276-291 | 16 | |
| α-helix | 295-297 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 50-51 | 2 | 4 |
| α-helix | 58-59 | 2 | |
| α-helix | 60-73 | 14 | |
| α-helix | 77-85 | 9 | |
| α-helix | 93-99 | 7 | |
| α-helix | 107-121 | 15 | |
| β-strand | 123 | 1 | 5 |
| β-strand | 128-129 | 2 | 4 |
| α-helix | 139-152 | 14 | |
| β-strand | 156 | 1 | 5 |
| α-helix | 158-169 | 12 | |
| β-strand | 176-186 | 11 | 6 |
| β-strand | 189-200 | 12 | 6 |
| β-strand | 203-207 | 5 | 6 |
| β-strand | 218-222 | 5 | 6 |
| α-helix | 225-237 | 13 | |
| α-helix | 241 | 1 | |
| β-strand | 242-248 | 7 | 6 |
| α-helix | 250-253 | 4 | |
| α-helix | 260-263 | 4 | |
| β-strand | 267-269 | 3 | 6 |
| α-helix | 271-273 | 3 | |
| α-helix | 276-292 | 17 | |
| α-helix | 295-297 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-59 | 33 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 29-59 | 31 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulinyl-Tyr carboxypeptidase 2 | A, B | protein | 355 | Mus musculus | Q8C5G2 (AlphaFold model) |
| Small vasohibin-binding protein | C, D | protein | 88 | Homo sapiens | Q8N300 (AlphaFold model) |
>6JZC_1 Tubulinyl-Tyr carboxypeptidase 2 (chains A, B) MTGSAADTHRCPHPKITKGTRSRSSHARPVSLATSGGSEEEDKDGGVLFHVNKSGFPIDS HTWERMWLHVAKVHPRGGEMVGAIRNAAFLAKPSIPQVPNYRLSMTIPDWLQAIQNYMKT LQYNHTGTQFFEIRKMRPLSGLMETAKEMTRESLPIKCLEAVILGIYLTNGQPSIERFPI SFKTYFSGNYFHHVVLGIYCNGYYGSLGMSRRAELMDKPLTFRTLSDLVFDFEDSYKKYL HTVKKVKIGLYVPHEPHSFQPIEWKQLVLNVSKMLRADIRKELEKYARDMRMKILKPASA HSPTQVRSRGKSLSPRRRQASPPRRLGRRDKSPALTEKKVADLGTLNEVGYQIRI
>6JZC_2 Small vasohibin-binding protein (chains C, D) MHHHHHHHHHHSGDEVDAGSGHMDPPARKEKTKVKESVSRVEKAKQKSAQQELKQRQRAE IYALNRVMTELEQQQFDEFCKQMQPPGE
Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer. Zhou, C., Yan, L., Zhang, W.H. et al. Nat Commun (2019) 10:3212-3212. DOI 10.1038/s41467-019-11277-8 · PubMed
Other PDB entries of the same protein (UniProt Q8C5G2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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