Current Protein Identity:P26441 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1CNT CILIARY NEUROTROPHIC FACTOR Deposited 1996-06-06 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain 1 1–187(187 aa)
Chain 4 1–187(187 aa)
Mutation:13 C-TERMINAL RESIDUES DELETED IN THIS CONSTRUCT Mutation:13 C-TERMINAL RESIDUES DELETED IN THIS CONSTRUCT SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.40 Å R-free 0.247
1CNT CILIARY NEUROTROPHIC FACTOR Deposited 1996-06-06 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain 2 1–187(187 aa)
Chain 3 1–187(187 aa)
Mutation:13 C-TERMINAL RESIDUES DELETED IN THIS CONSTRUCT Mutation:13 C-TERMINAL RESIDUES DELETED IN THIS CONSTRUCT SO4 SULFATE ION × 2 YB YTTERBIUM (III) ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.40 Å R-free 0.247
8D74 Cryo-EM structure of human CNTF signaling complex: model containing the interaction core region Deposited 2022-06-07 Assembly 1 Other combination Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain D 1–186(186 aa)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.03 Å