3S98: Human IFNAR1

human IFNAR1. Determined by X-ray diffraction at 1.9 Å resolution. Released 31 Aug 2011.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
1
Atoms
2,349
Mol. weight
35.86 kDa
Ligands
NAG
Released
31 Aug 2011

Explore 3S98 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3S98 contains 12 α-helices and 27 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: 12 helices, 27 β-strands

ElementResiduesLengthSheet
β-strand10-1451
β-strand17-2151
β-strand33-4082
β-strand47-4822
α-helix491
β-strand5512
β-strand59-6131
β-strand73-8082
β-strand85-8952
β-strand9312
α-helix95-984
β-strand10011
α-helix101-1044
β-strand105-11063
β-strand115-12063
β-strand137-14484
β-strand151-15664
β-strand159-16243
α-helix165-1662
β-strand170-179104
α-helix180-1823
β-strand184-18524
α-helix187-1915
β-strand192-19544
α-helix199-2002
α-helix203-2053
β-strand206-21385
β-strand216-22275
β-strand229-23686
α-helix237-2404
β-strand251-25226
α-helix254-2563
β-strand25916
β-strand263-26755
α-helix268-2703
β-strand275-28396
β-strand28816
α-helix289-2946
β-strand295-29846

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interferon alpha/beta receptor 1Aprotein306Homo sapiensP17181 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3S98_1 Interferon alpha/beta receptor 1 (chains A)
ADPLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTK
CNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHI
SPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAAL
LTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFL
KRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDT
EIQAFL

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O61

Primary citation

Structural linkage between ligand discrimination and receptor activation by type I interferons. Thomas, C., Moraga, I., Levin, D. et al. Cell (2011) 146:621-632. DOI 10.1016/j.cell.2011.06.048 · PubMed

Other PDB entries of the same protein (UniProt P17181 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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