1NBP: Interleukin-2

Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With 3-Mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-one. Determined by X-ray diffraction at 2.2 Å resolution. Released 18 Dec 2002.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
1
Atoms
1,057
Mol. weight
15.73 kDa
Ligands
MHC
Released
18 Dec 2002

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

Secondary structure: helices and β-sheets

1NBP contains 9 α-helices and 4 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: 9 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix7-2822
α-helix33-397
β-strand4411
β-strand4712
α-helix53-564
α-helix57-604
α-helix63-7210
α-helix82-9716
α-helix104-1063
β-strand10712
α-helix1081
β-strand11211
α-helix114-12916

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interleukin-2Aprotein133Homo sapiensP60568 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1NBP_1 Interleukin-2 (chains A)
APTSSSTKKTQLQLEHLLLDLQMILNGINNCKNPKLTRMLTFKFYMPKKATELKHLQCLE
EELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNR
WITFCQSIISTLT

Ligands and cofactors

IDNameFormulaCopies
MHC3-mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-oneC14 H16 N2 O S1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2. Hyde, J., Braisted, A.C., Randal, M. et al. Biochemistry (2003) 42:6475-6483. DOI 10.1021/bi034138g · 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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