2OIB: IRAK4 kinase domain apo form

Crystal structure of IRAK4 kinase domain apo form. Determined by X-ray diffraction at 2.0 Å resolution. Released 20 Mar 2007.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,747
Mol. weight: 135.82 kDa
Released: 20 Mar 2007

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

Secondary structure: helices and β-sheets

2OIB contains 76 α-helices and 69 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: 19 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	166-168	3	1
α-helix	170-176	7
β-strand	184	1	1
α-helix	185-187	3
β-strand	191-193	3	1
β-strand	200-205	6	1
β-strand	208-213	6	1
α-helix	223-239	17
β-strand	245	1	2
α-helix	246-247	2
β-strand	248-252	5	1
β-strand	259-263	5	1
β-strand	269	1	2
α-helix	270-275	6
α-helix	277-279	3
α-helix	280-284	5
α-helix	285-304	20
β-strand	307-308	2	3
α-helix	314-316	3
β-strand	317-319	3	2
β-strand	325-327	3	2
β-strand	334-335	2	3
β-strand	343-344	2	4
α-helix	352-354	3
α-helix	357-360	4
β-strand	363-364	2	4
α-helix	366-382	17
β-strand	387	1	5
β-strand	391	1	6
β-strand	395	1	5
α-helix	396-398	3
α-helix	399-404	6
α-helix	410-413	4
α-helix	423-436	14
α-helix	441-443	3
α-helix	445-446	2
α-helix	447-457	11

Chain B: 18 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	166-167	2	7
α-helix	170-176	7
β-strand	183	1	8
β-strand	190	1	8
β-strand	191-193	3	7
β-strand	199-205	7	7
β-strand	208-214	7	7
α-helix	225-239	15
β-strand	245	1	9
α-helix	246-247	2
β-strand	248-252	5	7
β-strand	259-263	5	7
β-strand	269	1	9
α-helix	270-274	5
α-helix	277-279	3
α-helix	280-284	5
α-helix	285-304	20
β-strand	307-308	2	10
α-helix	314-316	3
β-strand	317-319	3	9
β-strand	325-327	3	9
β-strand	334-335	2	10
β-strand	344	1	11
α-helix	352-354	3
α-helix	357-360	4
β-strand	363	1	11
α-helix	367-382	16
β-strand	387	1	12
β-strand	395	1	12
α-helix	396-398	3
α-helix	399-404	6
α-helix	410-413	4
α-helix	423-436	14
α-helix	441-443	3
α-helix	445-446	2
α-helix	447-458	12

Chain C: 20 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	166-167	2	13
α-helix	168-169	2
α-helix	170-176	7
α-helix	184-185	2
β-strand	199-205	7	13
β-strand	208-215	8	13
α-helix	225-239	15
β-strand	245	1	14
α-helix	246-247	2
β-strand	248-252	5	13
β-strand	258-263	6	13
β-strand	269	1	14
α-helix	270-274	5
α-helix	277-279	3
α-helix	280-284	5
α-helix	285-304	20
β-strand	308	1	15
α-helix	314-316	3
β-strand	317-319	3	14
β-strand	325-327	3	14
β-strand	334	1	15
β-strand	343-344	2	16
α-helix	352-354	3
α-helix	357-360	4
β-strand	363-364	2	16
α-helix	366-382	17
β-strand	387	1	17
β-strand	395	1	17
α-helix	396-398	3
α-helix	399-404	6
α-helix	410-413	4
α-helix	423-436	14
α-helix	441-443	3
α-helix	445-446	2
α-helix	447-457	11

Chain D: 19 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	163-165	3
β-strand	166-167	2	18
α-helix	168-169	2
α-helix	170-176	7
β-strand	184	1	18
β-strand	191-193	3	18
β-strand	199-205	7	18
β-strand	208-214	7	18
α-helix	224-239	16
β-strand	245	1	19
β-strand	248-252	5	18
β-strand	259-263	5	18
β-strand	269	1	19
α-helix	270-274	5
α-helix	277-279	3
α-helix	280-284	5
α-helix	285-304	20
β-strand	307-308	2	20
α-helix	314-316	3
β-strand	317-319	3	19
β-strand	325-327	3	19
β-strand	334-335	2	20
β-strand	343-344	2	21
α-helix	352-354	3
α-helix	357-360	4
β-strand	363-364	2	21
α-helix	367-382	16
β-strand	387	1	22
β-strand	391	1	6
β-strand	395	1	22
α-helix	396-398	3
α-helix	399-404	6
α-helix	410-413	4
α-helix	423-436	14
α-helix	441-443	3
α-helix	445-446	2
α-helix	447-457	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interleukin-1 receptor-associated kinase 4	A, B, C, D	protein	301	Homo sapiens	Q9NWZ3 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2OIB_1 Interleukin-1 receptor-associated kinase 4 (chains A, B, C, D)
VSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMV
DITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDG
TPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTAKISDFGLARASEKF
AQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDI
KEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTA
S

Primary citation

Cutting Edge: IL-1 Receptor-Associated Kinase 4 Structures Reveal Novel Features and Multiple Conformations. Kuglstatter, A., Villasenor, A.G., Shaw, D. et al. J Immunol (2007) 178:2641-2645. PubMed

Other PDB entries of the same protein (UniProt Q9NWZ3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6EGE 1.4 Å, Crystal structure of the unphosphorylated IRAK4 kinase domain Bound to a type I inhibitor
9NA5 1.73 Å, IRAK4 in Complex with Compound 24
6UYA 1.74 Å, Crystal structure of Compound 19 bound to IRAK4
8W3X 1.76 Å, Crystal structure of IRAK4 in complex with compound 6
6O95 1.77 Å, Structure of the IRAK4 kinase domain with compound 41
6O8U 1.8 Å, Crystal structure of IRAK4 in complex with compound 23
8UCC 1.8 Å, IRAK4 in complex with compound 20
5UIT 1.84 Å, Crystal structure of IRAK4 in complex with compound 14
8UCB 1.85 Å, IRAK4 in complex with compound 8
9R9K 1.87 Å, IRAK4 in complex with inhibitor
9R9G 1.88 Å, IRAK4 in complex with inhibitor
8SCE 1.89 Å, Crystal structure of IRAK4-HSA complexed with N-[(2R)-2-FLUORO-3-HYDROXY-3-METHYLBUTYL]-6…

Browse structure collections

About this viewer

MolViewer shows 2OIB directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.