Crystal structure of the ILK mutant (R371Q)/alpha-parvin core complex bound to gefitinib. Determined by X-ray diffraction at 1.5 Å resolution. Released 29 Oct 2025.
Explore 9D5H in 3D Show helices and sheets RCSB PDB PDBe
9D5H contains 25 α-helices and 11 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 | 190-192 | 3 | |
| β-strand | 194-202 | 9 | 1 |
| β-strand | 205-212 | 8 | 1 |
| β-strand | 215-222 | 8 | 1 |
| α-helix | 229-238 | 10 | |
| α-helix | 239-242 | 4 | |
| β-strand | 250-251 | 2 | 2 |
| β-strand | 255-257 | 3 | 1 |
| β-strand | 266-270 | 5 | 1 |
| β-strand | 276 | 1 | 2 |
| α-helix | 277-282 | 6 | |
| α-helix | 291-308 | 18 | |
| α-helix | 322-324 | 3 | |
| β-strand | 325-327 | 3 | 2 |
| β-strand | 333-336 | 4 | 2 |
| α-helix | 337-339 | 3 | |
| α-helix | 340-342 | 3 | |
| β-strand | 350 | 1 | 3 |
| α-helix | 353-355 | 3 | |
| α-helix | 358-361 | 4 | |
| α-helix | 365-367 | 3 | |
| α-helix | 370-387 | 18 | |
| α-helix | 397-406 | 10 | |
| α-helix | 411-414 | 4 | |
| α-helix | 419-428 | 10 | |
| α-helix | 433-435 | 3 | |
| α-helix | 437-438 | 2 | |
| α-helix | 439-449 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 258-276 | 19 | |
| α-helix | 277-279 | 3 | |
| α-helix | 294-304 | 11 | |
| β-strand | 307 | 1 | 3 |
| α-helix | 310-312 | 3 | |
| α-helix | 320-336 | 17 | |
| α-helix | 346-350 | 5 | |
| α-helix | 354-368 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Integrin-linked protein kinase | A | protein | 271 | Homo sapiens | Q13418 (AlphaFold model) |
| Alpha-parvin | B | protein | 129 | Homo sapiens | Q9NVD7 (AlphaFold model) |
>9D5H_1 Integrin-linked protein kinase (chains A) MNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPR LRIFSHPNVLPVLGACQSPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDM ARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQSPGRMYAPAWVAPEAL QKKPEDTNRQSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHV SKLMKICMNEDPAKRPKFDMIVPILEKMQDK
>9D5H_2 Alpha-parvin (chains B) GSHMDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLL EGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYN LFTKYRNVE
| ID | Name | Formula | Copies |
|---|---|---|---|
| B3P | 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-pr… | C11 H26 N2 O6 | 1 |
| IRE | Gefitinib | C22 H24 Cl F N4 O3 | 1 |
Crystal structure of the ILK mutant (R371Q)/alpha-parvin core complex bound to gefitinib. Fukdua, K., Qin, J. To be published.
Other PDB entries of the same protein (UniProt Q13418 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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