3S9D: Binary complex between IFNa2 and IFNAR2

binary complex between IFNa2 and IFNAR2. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Aug 2011.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,393
Mol. weight: 84.42 kDa
Released: 31 Aug 2011

Explore 3S9D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3S9D contains 28 α-helices and 32 β-strands across 4 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: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	9-21	13
α-helix	27-32	6
α-helix	40-42	3
α-helix	53-66	14
α-helix	70-75	6
α-helix	78-97	20
α-helix	115-132	18
α-helix	137-154	18

Chain B: 6 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	1
β-strand	22-28	7	1
α-helix	36-37	2
β-strand	38-45	8	2
α-helix	50-52	3
β-strand	53-54	2	2
α-helix	56-58	3
β-strand	61	1	2
β-strand	65-67	3	1
β-strand	79-86	8	2
β-strand	92-99	8	2
α-helix	101-104	4
β-strand	106-107	2	1
α-helix	108-110	3
β-strand	111-116	6	3
β-strand	121-126	6	3
β-strand	140-147	8	4
β-strand	150-154	5	4
β-strand	165-170	6	3
β-strand	178-186	9	4
α-helix	195-198	4
β-strand	199-202	4	4

Chain C: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	9-21	13
α-helix	27-32	6
α-helix	55-66	12
α-helix	70-75	6
α-helix	78-96	19
α-helix	118-132	15
α-helix	137-154	18

Chain D: 7 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	12-19	8	5
β-strand	22-29	8	5
α-helix	36-37	2
β-strand	38-45	8	6
α-helix	50-52	3
β-strand	53-54	2	6
α-helix	56-58	3
β-strand	61	1	6
β-strand	65-67	3	5
β-strand	79-87	9	6
β-strand	90-99	10	6
α-helix	101-104	4
β-strand	106-107	2	5
α-helix	108-110	3
β-strand	111-116	6	7
β-strand	121-126	6	7
β-strand	140-147	8	8
β-strand	150-154	5	8
β-strand	165-170	6	7
β-strand	178-186	9	8
α-helix	195-198	4
β-strand	199-202	4	8
α-helix	203-204	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interferon alpha-2	A, C	protein	168	Homo sapiens	P01563 (AlphaFold model)
Interferon alpha/beta receptor 2	B, D	protein	199	Homo sapiens	P48551 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>3S9D_1 Interferon alpha-2 (chains A, C)
ADPCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLA
AMIAQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSIL
AVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE

Sequence of entity 2 (B, D), FASTA

>3S9D_2 Interferon alpha/beta receptor 2 (chains B, D)
ADPESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKPEDLKVVKNCANTTRSFC
DLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNFWLAIDMSFEPPEFEIVGFTNHINVMVK
FPSIVEEELQFDLSLVIEEQSEGIVKKHKPEIKGNMSGNFTYIIDKLIPNTNYCVSVYLE
HSDEQAVIKSPLKCTLLPP

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 P01563 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9GVO 1.81 Å, type-I interferons autoantibodies pmab15 and pmab14 in complex with Interferon alpha-2
9GVL 2.01 Å, type-I interferons autoantibody pmab15 in complex with Interferon alpha-2
1RH2 2.9 Å, Recombinant human interferon-alpha 2B
4YPG 3.0 Å, Structural Insights Into the Neutralization Properties of a Human Anti-Interferon…
4Z5R 3.0 Å, Rontalizumab Fab bound to Interferon-a2
9GW5 4.0 Å, type-I interferon autoantibodies pmab3, pmab19 and pmab14 in complex with Interferon…
3SE3 4.0 Å, human IFNa2-IFNAR ternary complex
1ITF Interferon alpha-2A, NMR, 24 structures
2HYM NMR based Docking Model of the Complex between the Human Type I Interferon Receptor and…
2KZ1 Inter-molecular interactions in a 44 kDa interferon-receptor complex detected by…
2LAG Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of…
2LMS A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of…

Browse structure collections

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