1EMR: Human leukemia inhibitory factor

Crystal structure of human leukemia inhibitory factor (LIF). Determined by X-ray diffraction at 3.5 Å resolution. Released 21 Mar 2001.

Method
X-ray diffraction
Resolution
3.5 Å
Organism
Homo sapiens
Chains
1
Atoms
1,232
Mol. weight
17.52 kDa
Released
21 Mar 2001

Explore 1EMR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix26-4924
α-helix57-604
α-helix77-10529
α-helix110-13526
α-helix156-17722
α-helix178-1803

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Leukemia inhibitory factorAprotein159Homo sapiensP15018 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1EMR_1 LEUKEMIA INHIBITORY FACTOR (chains A)
LMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLEKLCGPNVTDFPPFHANGTEKAKLV
ELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLCRLCSKYHVGH
VDVTYGPDTSGKDVFQKKKLGCQLLGKYKQVISVLAQAF

Primary citation

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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