2KZ1: Interferon alpha-2

Inter-molecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric back-protonation and 2D NOESY. Determined by solution NMR. Released 23 Jun 2010.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 2,927
Mol. weight: 43.59 kDa
Released: 23 Jun 2010

Explore 2KZ1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KZ1 contains 8 α-helices and 15 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, 0 β-strands

Element	Residues	Length
α-helix	10-20	11
α-helix	26-28	3
α-helix	53-67	15
α-helix	72-74	3
α-helix	78-100	23
α-helix	111-132	22
α-helix	137-159	23

Chain B: 1 helix, 15 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	1
β-strand	22-28	7	1
β-strand	38-44	7	2
β-strand	53-54	2	2
β-strand	61	1	2
β-strand	65-67	3	1
β-strand	78-86	9	2
β-strand	91-100	10	2
β-strand	111-116	6	3
β-strand	121-126	6	3
α-helix	132-134	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
β-strand	199-202	4	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interferon alpha-2	A	protein	165	Homo sapiens	P01563 (AlphaFold model)
Soluble IFN alpha/beta receptor	B	protein	212	Homo sapiens	P48551 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2KZ1_1 Interferon alpha-2 (chains A)
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMI
QQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVR
KYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE

Sequence of entity 2 (B), FASTA

>2KZ1_2 Soluble IFN alpha/beta receptor (chains B)
SYDSPDYTDESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKPEDLKVVKNCAN
TTRSFCDLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNFWLAIDMSFEPPEFEIVGFTNH
INVMVKFPSIVEEELQFDLSLVIEEQSEGIVKKHKPEIKGNMSGNFTYIIDKLIPNTNYC
VSVYLEHSDEQAVIKSPLKCTLLPPGQESEFS

Primary citation

Intermolecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric reverse-protonation and two-dimensional NOESY. Nudelman, I., Akabayov, S.R., Schnur, E. et al. Biochemistry (2010) 49:5117-5133. DOI 10.1021/bi100041f · 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
3S9D 2.0 Å, binary complex between IFNa2 and IFNAR2
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…
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…

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