5JEK: Phosphorylated MAVS

Phosphorylated MAVS in complex with IRF-3. Determined by X-ray diffraction at 2.4 Å resolution. Released 15 Jun 2016.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,965
Mol. weight: 57.56 kDa
Released: 15 Jun 2016

Explore 5JEK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5JEK contains 20 α-helices and 36 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: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	191-196	6
β-strand	202	1	1
β-strand	204-210	7	2
β-strand	213-220	8	2
β-strand	226-229	4	3
β-strand	236	1	4
β-strand	238	1	4
β-strand	241-244	4	3
α-helix	245-247	3
α-helix	248-250	3
α-helix	255-266	12
β-strand	272-277	6	3
β-strand	280-285	6	3
β-strand	289	1	5
β-strand	291-296	6	2
β-strand	309-310	2	2
α-helix	311-312	2
β-strand	318-321	4	3
α-helix	322-333	12
α-helix	339-341	3
β-strand	343-348	6	2
α-helix	358-360	3
β-strand	363-369	7	2
α-helix	370-382	13
β-strand	388-391	4	6
β-strand	395	1	1
β-strand	401-404	4	6
α-helix	405-417	13

Chain B: 9 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	191-195	5
β-strand	202	1	7
β-strand	203-210	8	8
β-strand	213-221	9	8
β-strand	226-229	4	9
β-strand	241-244	4	9
α-helix	245-247	3
α-helix	255-265	11
β-strand	272-277	6	9
β-strand	280-285	6	9
β-strand	289	1	10
β-strand	291-296	6	8
β-strand	309-310	2	8
β-strand	317-321	5	9
α-helix	322-333	12
α-helix	339-341	3
β-strand	343-348	6	8
α-helix	358-360	3
β-strand	363-369	7	8
α-helix	370-380	11
α-helix	381-383	3
β-strand	389-391	3	11
β-strand	395	1	7
β-strand	401-403	3	11
α-helix	405-416	12

Chain C: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	441	1	5
α-helix	442-444	3

Chain D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	441	1	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interferon regulatory factor 3	A, B	protein	242	Homo sapiens	Q14653 (AlphaFold model)
MAVS peptide	C, D	protein	18	Homo sapiens	Q7Z434 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5JEK_1 Interferon regulatory factor 3 (chains A, B)
SEFENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTL
PDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGH
GPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMV
KVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPG
ES

Sequence of entity 2 (C, D), FASTA

>5JEK_2 MAVS peptide (chains C, D)
SGCFEDLAISASTSLGWG

Primary citation

Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. Zhao, B., Shu, C., Gao, X. et al. Proc Natl Acad Sci U S A (2016) 113:E3403-E3412. DOI 10.1073/pnas.1603269113 · PubMed

Other PDB entries of the same protein (UniProt Q14653 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6SJA 1.5 Å, Structure of HPV16 E6 oncoprotein in complex with IRF3 LxxLL motif
5JEL 1.6 Å, Phosphorylated TRIF in complex with IRF-3
7JFL 1.68 Å, Crystal structure of human phosphorylated IRF-3 bound to CBP
5JEO 1.72 Å, Phosphorylated Rotavirus NSP1 in complex with IRF-3
6SIV 1.75 Å, Structure of HPV16 E6 oncoprotein in complex with mutant IRF3 LxxLL motif
3A77 1.8 Å, The crystal structure of phosphorylated IRF-3
5JEJ 2.0 Å, Phosphorylated STING in complex with IRF-3 CTD
1QWT 2.1 Å, Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain
1J2F 2.3 Å, X-ray crystal structure of IRF-3 and its functional implications
3QU6 2.3 Å, Crystal structure of IRF-3 DBD free form
2PI0 2.31 Å, Crystal Structure of IRF-3 bound to the PRDIII-I regulatory element of the human…
1ZOQ 2.37 Å, IRF3-CBP complex

Browse structure collections

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