Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized by carrier-driven crystallization in fusion with the macro domain of human histone macroH2A1.1. Determined by X-ray diffraction at 3.29 Å resolution. Released 9 Nov 2016.
Explore 5LNC in 3D Show helices and sheets RCSB PDB PDBe
5LNC contains 28 α-helices and 16 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 | 4-8 | 5 | |
| α-helix | 13-15 | 3 | |
| α-helix | 22-35 | 14 | |
| α-helix | 42-87 | 46 | |
| β-strand | 89 | 1 | 1 |
| β-strand | 91 | 1 | 1 |
| α-helix | 95-137 | 43 | |
| α-helix | 143-151 | 9 | |
| α-helix | 160-178 | 19 | |
| β-strand | 188-191 | 4 | 2 |
| β-strand | 197-201 | 5 | 2 |
| α-helix | 205-207 | 3 | |
| β-strand | 212-217 | 6 | 2 |
| α-helix | 225-250 | 26 | |
| α-helix | 253-254 | 2 | |
| β-strand | 258-262 | 5 | 2 |
| β-strand | 270-275 | 6 | 2 |
| α-helix | 276-278 | 3 | |
| α-helix | 284-301 | 18 | |
| β-strand | 306-309 | 4 | 2 |
| α-helix | 321-338 | 18 | |
| β-strand | 346-350 | 5 | 2 |
| α-helix | 354-365 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-8 | 5 | |
| α-helix | 13-15 | 3 | |
| α-helix | 22-35 | 14 | |
| α-helix | 42-88 | 47 | |
| α-helix | 96-137 | 42 | |
| α-helix | 143-151 | 9 | |
| α-helix | 160-177 | 18 | |
| β-strand | 186-191 | 6 | 3 |
| β-strand | 197-201 | 5 | 3 |
| α-helix | 205-207 | 3 | |
| β-strand | 212-217 | 6 | 3 |
| α-helix | 225-250 | 26 | |
| α-helix | 253-254 | 2 | |
| β-strand | 258-262 | 5 | 3 |
| β-strand | 270-275 | 6 | 3 |
| α-helix | 276-278 | 3 | |
| α-helix | 284-301 | 18 | |
| β-strand | 306-309 | 4 | 3 |
| α-helix | 321-338 | 18 | |
| β-strand | 346-350 | 5 | 3 |
| α-helix | 354-365 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar transporter chaperone 4,Core histone macro-H2A.1 | A, B | protein | 374 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiens | O75367 (AlphaFold model), P47075 (AlphaFold model) |
>5LNC_1 Vacuolar transporter chaperone 4,Core histone macro-H2A.1 (chains A, B) MKFGEHLSKSLIRQYSYYYISYDDLKTELEDNLSKNNGQWTQELETDFLESLEIELDKVY TFCKVKHSEVFRRVKEVQEQVQHTVRLLDSNNPPTQLDFEILEEELSDIIADVHDLAKFS RLNYTGFQKIIKKHDKKTGFILKPVFQVRLDSKPFFKENYDELVVKISQLYDIARTSGAG SDGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFV EAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALAD DKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIY VQEMAKLEHHHHHH
The macro domain as fusion tag for carrier-driven crystallization. Wild, R., Hothorn, M. Protein Sci (2017) 26:365-374. DOI 10.1002/pro.3073 · PubMed
Other PDB entries of the same protein (UniProt O75367 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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