Human Inositol (1,4,5)-trisphosphate 3-kinase substituted with selenomethionine. Determined by X-ray diffraction at 1.8 Å resolution. Released 9 Sept 2004.
Explore 1W2F in 3D Show helices and sheets RCSB PDB PDBe
1W2F contains 28 α-helices and 26 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 | 188-191 | 4 | |
| β-strand | 199-200 | 2 | 1 |
| β-strand | 206-210 | 5 | 1 |
| α-helix | 213-223 | 11 | |
| α-helix | 226-230 | 5 | |
| β-strand | 234-240 | 7 | 1 |
| β-strand | 243-249 | 7 | 1 |
| β-strand | 259-265 | 7 | 2 |
| α-helix | 272-280 | 9 | |
| β-strand | 284-285 | 2 | 3 |
| α-helix | 286-295 | 10 | |
| α-helix | 302-307 | 6 | |
| β-strand | 310-311 | 2 | 3 |
| α-helix | 312-322 | 11 | |
| α-helix | 325-328 | 4 | |
| β-strand | 330-336 | 7 | 2 |
| β-strand | 342-343 | 2 | 2 |
| α-helix | 352-363 | 12 | |
| α-helix | 367-384 | 18 | |
| α-helix | 388-391 | 4 | |
| β-strand | 393-396 | 4 | 4 |
| β-strand | 399-404 | 6 | 2 |
| β-strand | 410-415 | 6 | 2 |
| β-strand | 419-422 | 4 | 4 |
| α-helix | 423 | 1 | |
| α-helix | 434-435 | 2 | |
| α-helix | 444-459 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 188-191 | 4 | |
| β-strand | 198-200 | 3 | 5 |
| β-strand | 206-210 | 5 | 5 |
| α-helix | 213-223 | 11 | |
| α-helix | 226-230 | 5 | |
| β-strand | 234-240 | 7 | 5 |
| β-strand | 243-249 | 7 | 5 |
| β-strand | 259-265 | 7 | 2 |
| α-helix | 272-280 | 9 | |
| β-strand | 284-285 | 2 | 6 |
| α-helix | 286-295 | 10 | |
| α-helix | 302-307 | 6 | |
| β-strand | 310-311 | 2 | 6 |
| α-helix | 312-322 | 11 | |
| α-helix | 325-328 | 4 | |
| β-strand | 330-336 | 7 | 2 |
| β-strand | 342-343 | 2 | 2 |
| α-helix | 352-363 | 12 | |
| α-helix | 367-386 | 20 | |
| α-helix | 388-392 | 5 | |
| β-strand | 393-396 | 4 | 7 |
| β-strand | 399-404 | 6 | 2 |
| β-strand | 410-415 | 6 | 2 |
| β-strand | 419-422 | 4 | 7 |
| α-helix | 423 | 1 | |
| α-helix | 434-435 | 2 | |
| α-helix | 444-460 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Inositol-trisphosphate 3-kinase A | A, B | protein | 276 | HOMO SAPIENS | P23677 (AlphaFold model) |
>1W2F_1 INOSITOL-TRISPHOSPHATE 3-KINASE A (chains A, B) MSWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVERDGESY LQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEH AQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFEEFVQG DEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKTTPLPD GQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER
Structure of a Human Inositol 1,4,5-Trisphosphate 3-Kinase; Substrate Binding Reveals Why It is not a Phosphoinositide 3-Kinase. Gonzalez, B., Schell, M.J., Letcher, A.J. et al. Mol Cell (2004) 15:689. DOI 10.1016/J.MOLCEL.2004.08.004 · PubMed
Other PDB entries of the same protein (UniProt P23677 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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