1IGL: Insulin-like growth factor II

Solution structure of human insulin-like growth factor II relationship to receptor and binding protein interactions. Determined by solution NMR. Released 14 Feb 1995.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
521
Mol. weight
7.48 kDa
Released
14 Feb 1995

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

Secondary structure: helices and β-sheets

1IGL contains 3 α-helices and 2 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: 3 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix14-207
β-strand2611
α-helix44-485
α-helix54-596
β-strand6011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Insulin-like growth factor IIAprotein67Homo sapiensP01344 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1IGL_1 INSULIN-LIKE GROWTH FACTOR II (chains A)
AYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYC
ATPAKSE

Primary citation

Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions. Torres, A.M., Forbes, B.E., Aplin, S.E. et al. J Mol Biol (1995) 248:385-401. PubMed

Other PDB entries of the same protein (UniProt P01344 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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