1M49: Human Interleukin-2

Crystal Structure of Human Interleukin-2 Complexed with SP-1985. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Jul 2002.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
2
Atoms
2,134
Mol. weight
32 kDa
Ligands
CMM
Released
31 Jul 2002

Explore 1M49 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M49 contains 16 α-helices and 8 β-strands across 2 chains. 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: 7 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix5-2824
α-helix33-408
β-strand4411
β-strand4712
α-helix53-564
α-helix57-604
α-helix63-7210
α-helix82-9716
β-strand10712
β-strand11211
α-helix114-13118
Chain B: 9 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix5-2824
α-helix36-394
β-strand4413
β-strand4714
α-helix53-564
α-helix57-604
α-helix63-7210
α-helix82-9615
α-helix104-1063
β-strand10714
α-helix1081
β-strand11213
α-helix114-13118

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
interleukin-2A, Bprotein133Homo sapiensP60568 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1M49_1 interleukin-2 (chains A, B)
APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLE
EELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNR
WITFCQSIISTLT

Ligands and cofactors

IDNameFormulaCopies
CMM2-[2-(1-carbamimidoyl-piperidin-3-yl)-acetylamino]-3-{4-[2-(3-oxalyl-1H-indol-7…C30 H35 N5 O62

Primary citation

Binding of small molecules to an adaptive protein-protein interface. Arkin, M.A., Randal, M., DeLano, W.L. et al. Proc Natl Acad Sci U S A (2003) 100:1603-1608. DOI 10.1073/pnas.252756299 · PubMed

Other PDB entries of the same protein (UniProt P60568 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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