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 2.13 Å resolution. Released 27 Apr 2016.
Explore 5IIT in 3D Show helices and sheets RCSB PDB PDBe
5IIT contains 52 α-helices and 36 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 |
|---|---|---|---|
| α-helix | 15-18 | 4 | |
| α-helix | 21-35 | 15 | |
| α-helix | 42-89 | 48 | |
| β-strand | 95 | 1 | 1 |
| α-helix | 96-138 | 43 | |
| α-helix | 143-152 | 10 | |
| β-strand | 157 | 1 | 2 |
| α-helix | 160-175 | 16 | |
| α-helix | 184 | 1 | |
| β-strand | 185-191 | 7 | 3 |
| β-strand | 197-202 | 6 | 3 |
| α-helix | 205-207 | 3 | |
| β-strand | 212-216 | 5 | 3 |
| α-helix | 226-250 | 25 | |
| α-helix | 253-254 | 2 | |
| β-strand | 258-262 | 5 | 3 |
| β-strand | 270-274 | 5 | 3 |
| α-helix | 276-278 | 3 | |
| α-helix | 284-301 | 18 | |
| β-strand | 306-309 | 4 | 3 |
| α-helix | 321-338 | 18 | |
| β-strand | 346-351 | 6 | 3 |
| α-helix | 354-366 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-18 | 4 | |
| α-helix | 21-35 | 15 | |
| α-helix | 42-89 | 48 | |
| β-strand | 95 | 1 | 4 |
| α-helix | 96-138 | 43 | |
| α-helix | 143-152 | 10 | |
| β-strand | 157 | 1 | 5 |
| α-helix | 160-175 | 16 | |
| α-helix | 184 | 1 | |
| β-strand | 185-191 | 7 | 6 |
| β-strand | 197-202 | 6 | 6 |
| α-helix | 205-207 | 3 | |
| β-strand | 212-216 | 5 | 6 |
| α-helix | 225-250 | 26 | |
| α-helix | 253-254 | 2 | |
| β-strand | 258-262 | 5 | 6 |
| β-strand | 270-274 | 5 | 6 |
| α-helix | 276-278 | 3 | |
| α-helix | 284-301 | 18 | |
| β-strand | 306-309 | 4 | 6 |
| α-helix | 321-338 | 18 | |
| β-strand | 346-351 | 6 | 6 |
| α-helix | 354-366 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-18 | 4 | |
| α-helix | 21-35 | 15 | |
| α-helix | 42-89 | 48 | |
| β-strand | 95 | 1 | 5 |
| α-helix | 96-138 | 43 | |
| α-helix | 143-152 | 10 | |
| β-strand | 157 | 1 | 4 |
| α-helix | 160-175 | 16 | |
| α-helix | 184 | 1 | |
| β-strand | 185-191 | 7 | 7 |
| β-strand | 197-202 | 6 | 7 |
| β-strand | 212-216 | 5 | 7 |
| α-helix | 226-250 | 25 | |
| β-strand | 258-262 | 5 | 7 |
| β-strand | 270-274 | 5 | 7 |
| α-helix | 276-278 | 3 | |
| α-helix | 284-301 | 18 | |
| β-strand | 306-309 | 4 | 7 |
| α-helix | 321-338 | 18 | |
| β-strand | 346-350 | 5 | 7 |
| α-helix | 354-366 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-18 | 4 | |
| α-helix | 21-35 | 15 | |
| α-helix | 42-89 | 48 | |
| β-strand | 95 | 1 | 2 |
| α-helix | 96-138 | 43 | |
| α-helix | 143-152 | 10 | |
| β-strand | 157 | 1 | 1 |
| α-helix | 160-175 | 16 | |
| α-helix | 184 | 1 | |
| β-strand | 185-191 | 7 | 8 |
| β-strand | 197-202 | 6 | 8 |
| β-strand | 212-217 | 6 | 8 |
| α-helix | 225-250 | 26 | |
| β-strand | 258-262 | 5 | 8 |
| β-strand | 270-275 | 6 | 8 |
| α-helix | 276-278 | 3 | |
| α-helix | 284-301 | 18 | |
| β-strand | 306-309 | 4 | 8 |
| α-helix | 321-338 | 18 | |
| β-strand | 346-350 | 5 | 8 |
| α-helix | 354-366 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar transporter chaperone 4,Core histone macro-H2A.1 | A, B, C, D | protein | 374 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiens | O75367 (AlphaFold model), P47075 (AlphaFold model) |
>5IIT_1 Vacuolar transporter chaperone 4,Core histone macro-H2A.1 (chains A, B, C, D) MKFGEHLSKSLIRQYSYYYISYDDLKTELEDNLSKNNGQWTQELETDFLESLEIELDKVY TFCKVKHSEVFRRVKEVQEQVQHTVRLLDSNNPPTQLDFEILEEELSDIIADVHDLAKFS RLNYTGFQKIIKKHDKKTGFILKPVFQVRLDSKPFFKENYDELVVKISQLYDIARTSGAG SDGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFV EAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALAD DKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIY VQEMAKLEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
Water and common crystallization additives (EDO, SO4, MES) are not listed.
Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains. Wild, R., Gerasimaite, R., Jung, J.Y. et al. Science (2016) 352:986-990. DOI 10.1126/science.aad9858 · 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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