Crystal structure of leukemia inhibitory factor in complex with gp130. Determined by X-ray diffraction at 2.5 Å resolution. Released 14 Oct 2003.
Explore 1PVH in 3D Show helices and sheets RCSB PDB PDBe
1PVH contains 33 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 | 103-107 | 5 | |
| β-strand | 108-113 | 6 | 1 |
| β-strand | 114-115 | 2 | 2 |
| α-helix | 119-120 | 2 | |
| β-strand | 121-125 | 5 | 1 |
| β-strand | 135-141 | 7 | 3 |
| β-strand | 146 | 1 | 3 |
| α-helix | 147-149 | 3 | |
| β-strand | 150-151 | 2 | 3 |
| α-helix | 152-153 | 2 | |
| β-strand | 159-161 | 3 | 1 |
| α-helix | 165-166 | 2 | |
| β-strand | 172-180 | 9 | 3 |
| β-strand | 183-186 | 4 | 3 |
| β-strand | 190-192 | 3 | 3 |
| α-helix | 194-197 | 4 | |
| β-strand | 198-199 | 2 | 2 |
| α-helix | 200-203 | 4 | |
| β-strand | 204-209 | 6 | 4 |
| β-strand | 217-223 | 7 | 4 |
| α-helix | 226-229 | 4 | |
| β-strand | 233-241 | 9 | 5 |
| β-strand | 248-249 | 2 | 5 |
| α-helix | 252-255 | 4 | |
| β-strand | 261-265 | 5 | 4 |
| α-helix | 267-268 | 2 | |
| β-strand | 272-281 | 10 | 5 |
| α-helix | 288-291 | 4 | |
| β-strand | 295-298 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-19 | 3 | |
| α-helix | 22-48 | 27 | |
| α-helix | 56-59 | 4 | |
| α-helix | 76-104 | 29 | |
| α-helix | 109-135 | 27 | |
| α-helix | 155-177 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 103-107 | 5 | |
| β-strand | 108-113 | 6 | 6 |
| β-strand | 114-115 | 2 | 7 |
| α-helix | 119-120 | 2 | |
| β-strand | 121-125 | 5 | 6 |
| β-strand | 135-142 | 8 | 8 |
| β-strand | 145-146 | 2 | 8 |
| α-helix | 147-149 | 3 | |
| β-strand | 150-151 | 2 | 8 |
| α-helix | 152-153 | 2 | |
| β-strand | 159-161 | 3 | 6 |
| α-helix | 165-166 | 2 | |
| β-strand | 172-180 | 9 | 8 |
| β-strand | 183-186 | 4 | 8 |
| β-strand | 190-192 | 3 | 8 |
| α-helix | 194-197 | 4 | |
| β-strand | 198-199 | 2 | 7 |
| α-helix | 200-203 | 4 | |
| β-strand | 204-209 | 6 | 9 |
| β-strand | 217-223 | 7 | 9 |
| α-helix | 226-229 | 4 | |
| β-strand | 233-241 | 9 | 10 |
| β-strand | 248-249 | 2 | 10 |
| α-helix | 252-255 | 4 | |
| β-strand | 261-265 | 5 | 9 |
| α-helix | 267-268 | 2 | |
| β-strand | 272-281 | 10 | 10 |
| α-helix | 288-291 | 4 | |
| β-strand | 295-298 | 4 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-48 | 27 | |
| α-helix | 56-59 | 4 | |
| α-helix | 76-104 | 29 | |
| α-helix | 109-135 | 27 | |
| α-helix | 155-178 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-6 receptor beta chain | A, C | protein | 201 | Homo sapiens | P40189 (AlphaFold model) |
| Leukemia inhibitory factor | B, D | protein | 169 | Homo sapiens | P15018 (AlphaFold model) |
>1PVH_1 Interleukin-6 receptor beta chain (chains A, C) GLPPEKPKNLSCIVNEGKKMRCEWDGGRETHLETNFTLKSEWATHKFADCKAKRDTPTSC TVDYSTVYFVNIEVWVEAENALGKVTSDHINFDPVYKVKPNPPHNLSVINSEELSSILKL TWTNPSIKSVIILKYNIQYRTKDASTWSQIPPEDTASTRSSFTVQDLKPFTEYVFRIRCM KEDGKGYWSDWSEEASGITYE
>1PVH_2 Leukemia inhibitory factor (chains B, D) CAIRHPCHNNLMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLDKLCGPNVTDFPPFH ANGTEKAKLVELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLC RLCSKYHVGHVDVTYGPDTSGKDVFQKKKLGCQLLGKYKQIIAVLAQAF
Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130. Boulanger, M.J., Bankovich, A.J., Kortemme, T. et al. Mol Cell (2003) 12:577-589. DOI 10.1016/S1097-2765(03)00365-4 · PubMed
Other PDB entries of the same protein (UniProt P40189 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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