IGF-1RK in complex with ligand MSC1609119A-1. Determined by X-ray diffraction at 1.79 Å resolution. Released 29 Sept 2010.
Explore 3LW0 in 3D Show helices and sheets RCSB PDB PDBe
3LW0 contains 80 α-helices and 48 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 |
|---|---|---|---|
| β-strand | 993 | 1 | 1 |
| α-helix | 996-998 | 3 | |
| β-strand | 999-1007 | 9 | 1 |
| β-strand | 1012-1022 | 11 | 1 |
| β-strand | 1025-1034 | 10 | 1 |
| α-helix | 1041-1054 | 14 | |
| β-strand | 1062 | 1 | 2 |
| α-helix | 1063-1064 | 2 | |
| β-strand | 1065-1069 | 5 | 1 |
| β-strand | 1076-1080 | 5 | 1 |
| β-strand | 1086 | 1 | 2 |
| α-helix | 1087-1093 | 7 | |
| α-helix | 1109-1128 | 20 | |
| α-helix | 1138-1140 | 3 | |
| β-strand | 1141-1143 | 3 | 2 |
| β-strand | 1149-1151 | 3 | 2 |
| α-helix | 1162-1164 | 3 | |
| β-strand | 1166 | 1 | 3 |
| β-strand | 1174 | 1 | 3 |
| α-helix | 1176-1178 | 3 | |
| α-helix | 1181-1186 | 6 | |
| α-helix | 1191-1207 | 17 | |
| α-helix | 1210-1211 | 2 | |
| α-helix | 1218-1226 | 9 | |
| α-helix | 1231-1234 | 4 | |
| α-helix | 1239-1248 | 10 | |
| α-helix | 1253-1255 | 3 | |
| α-helix | 1257-1258 | 2 | |
| α-helix | 1259-1266 | 8 | |
| α-helix | 1267-1269 | 3 | |
| α-helix | 1271 | 1 | |
| α-helix | 1274-1277 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 993 | 1 | 7 |
| α-helix | 996-998 | 3 | |
| β-strand | 999-1007 | 9 | 7 |
| β-strand | 1012-1022 | 11 | 7 |
| β-strand | 1025-1034 | 10 | 7 |
| α-helix | 1041-1054 | 14 | |
| β-strand | 1062 | 1 | 8 |
| α-helix | 1063-1064 | 2 | |
| β-strand | 1065-1069 | 5 | 7 |
| β-strand | 1076-1080 | 5 | 7 |
| β-strand | 1085-1086 | 2 | 8 |
| α-helix | 1087-1093 | 7 | |
| α-helix | 1109-1128 | 20 | |
| α-helix | 1138-1140 | 3 | |
| β-strand | 1141-1143 | 3 | 8 |
| β-strand | 1149-1151 | 3 | 8 |
| α-helix | 1162-1164 | 3 | |
| β-strand | 1166 | 1 | 9 |
| β-strand | 1174 | 1 | 9 |
| α-helix | 1176-1178 | 3 | |
| α-helix | 1181-1186 | 6 | |
| α-helix | 1191-1207 | 17 | |
| α-helix | 1210-1211 | 2 | |
| α-helix | 1218-1226 | 9 | |
| α-helix | 1231-1234 | 4 | |
| α-helix | 1239-1248 | 10 | |
| α-helix | 1253-1255 | 3 | |
| α-helix | 1257-1258 | 2 | |
| α-helix | 1259-1266 | 8 | |
| α-helix | 1267-1269 | 3 | |
| α-helix | 1271 | 1 | |
| α-helix | 1274-1277 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Insulin-like growth factor 1 receptor | A, B, C, D | protein | 304 | Homo sapiens | P08069 (AlphaFold model) |
>3LW0_1 Insulin-like growth factor 1 receptor (chains A, B, C, D) AADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMR ERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPAMANNP VLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYE TDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGLSNEQVL RFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYS EENK
| ID | Name | Formula | Copies |
|---|---|---|---|
| CCX | 3-cyano-N-{1-[4-(5-cyano-1H-indol-3-yl)butyl]piperidin-4-yl}-1H-indole-7-carbox… | C28 H28 N6 O | 8 |
Water and common crystallization additives (GOL) are not listed.
Allosteric IGF-1R Inhibitors. Heinrich, T., Gradler, U., Bottcher, H. et al. ACS Med Chem Lett (2010) 1:199-203. DOI 10.1021/ml100044h · PubMed
Other PDB entries of the same protein (UniProt P08069 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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