Crystal structure of human leukemia inhibitory factor (LIF). Determined by X-ray diffraction at 3.5 Å resolution. Released 21 Mar 2001.
Explore 1EMR in 3D Show helices and sheets RCSB PDB PDBe
1EMR contains 6 α-helices and 0 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 | 26-49 | 24 | |
| α-helix | 57-60 | 4 | |
| α-helix | 77-105 | 29 | |
| α-helix | 110-135 | 26 | |
| α-helix | 156-177 | 22 | |
| α-helix | 178-180 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Leukemia inhibitory factor | A | protein | 159 | Homo sapiens | P15018 (AlphaFold model) |
>1EMR_1 LEUKEMIA INHIBITORY FACTOR (chains A) LMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLEKLCGPNVTDFPPFHANGTEKAKLV ELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLCRLCSKYHVGH VDVTYGPDTSGKDVFQKKKLGCQLLGKYKQVISVLAQAF
Species Variation in Receptor Binding Site Revealed by the Medium Resolution X-ray Structure of Human Leukemia Inhibitory Factor. Robinson, R.C., Heath, J.K., Hawkins, N. et al. To be published.
Other PDB entries of the same protein (UniProt P15018 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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