Crystal structure of the apo F1174L anaplastic lymphoma kinase catalytic domain. Determined by X-ray diffraction at 1.75 Å resolution. Released 29 Aug 2012.
Explore 4FNW in 3D Show helices and sheets RCSB PDB PDBe
4FNW contains 21 α-helices and 12 β-strands across 1 chain. 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 | 1087-1092 | 6 | |
| β-strand | 1096-1098 | 3 | 1 |
| β-strand | 1101-1103 | 3 | 1 |
| α-helix | 1105-1107 | 3 | |
| β-strand | 1110 | 1 | 2 |
| α-helix | 1111-1112 | 2 | |
| α-helix | 1113-1115 | 3 | |
| β-strand | 1116-1121 | 6 | 2 |
| β-strand | 1130-1135 | 6 | 2 |
| α-helix | 1144 | 1 | |
| β-strand | 1145-1151 | 7 | 2 |
| α-helix | 1158-1173 | 16 | |
| β-strand | 1179 | 1 | 3 |
| β-strand | 1182-1186 | 5 | 2 |
| β-strand | 1193-1197 | 5 | 2 |
| β-strand | 1202-1203 | 2 | 3 |
| α-helix | 1204-1210 | 7 | |
| α-helix | 1223-1242 | 20 | |
| α-helix | 1252-1254 | 3 | |
| β-strand | 1255-1257 | 3 | 3 |
| β-strand | 1266-1268 | 3 | 3 |
| α-helix | 1272-1278 | 7 | |
| α-helix | 1293-1295 | 3 | |
| α-helix | 1298-1303 | 6 | |
| α-helix | 1308-1323 | 16 | |
| α-helix | 1327-1328 | 2 | |
| α-helix | 1335-1343 | 9 | |
| α-helix | 1348-1351 | 4 | |
| α-helix | 1356-1365 | 10 | |
| α-helix | 1370-1372 | 3 | |
| α-helix | 1376-1388 | 13 | |
| α-helix | 1390-1393 | 4 | |
| α-helix | 1395-1401 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ALK tyrosine kinase receptor | A | protein | 327 | Homo sapiens | Q9UM73 (AlphaFold model) |
>4FNW_1 ALK tyrosine kinase receptor (chains A) RTSTIMTDYNPNYSFAGKTSSISDLKEVPRKNITLIRGLGHGAFGEVYEGQVSGMPNDPS PLQVAVKTLPEVCSEQDELDFLMEALIISKLNHQNIVRCIGVSLQSLPRFILLELMAGGD LKSFLRETRPRPSQPSSLAMLDLLHVARDIACGCQYLEENHFIHRDIAARNCLLTCPGPG RVAKIGDFGMARDIYRASYYRKGGCAMLPVKWMPPEAFMEGIFTSKTDTWSFGVLLWEIF SLGYMPYPSKSNQEVLEFVTSGGRMDPPKNCPGPVYRIMTQCWQHQPEDRPNFAIILERI EYCTQDPDVINTALPIEYGPLVEEEEK
The R1275Q Neuroblastoma Mutant and Certain ATP-competitive Inhibitors Stabilize Alternative Activation Loop Conformations of Anaplastic Lymphoma Kinase. Epstein, L.F., Chen, H., Emkey, R. et al. J Biol Chem (2012) 287:37447-37457. DOI 10.1074/jbc.M112.391425 · PubMed
Other PDB entries of the same protein (UniProt Q9UM73 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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