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Crystal structure of human leukemia inhibitory factor (lif)

Analyse Crystal structure of human leukemia inhibitory factor (lif) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EMR
Type
protein
Length
159 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Leukemia inhibitory factor
UniProt
P15018
Pockets
1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALeukemia inhibitory factorprotein15968% helix, 0% strandP15018

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.540.8417empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1EMR · Crystal structure of human leukemia inhibitory factor (lif) · the same entry in another collection · chain A against A, TM-score 1.00
  • P15018 · AlphaFold monomer V2.0 prediction for leukemia inhibitory factor (P15018) · a predicted model of the same protein · chain A against A, TM-score 0.98

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