3WO2: Human interleukin-18

Crystal structure of human interleukin-18. Determined by X-ray diffraction at 2.33 Å resolution. Released 17 Dec 2014.

Method: X-ray diffraction
Resolution: 2.33 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,733
Mol. weight: 80.72 kDa
Ligands: CPS
Released: 17 Dec 2014

Explore 3WO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3WO2 contains 26 α-helices and 52 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.

Chains A and D: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	2-13	12	1
α-helix	18	1
β-strand	19-22	4	1
β-strand	28-31	4	1
α-helix	35-40	6
α-helix	42-45	4
β-strand	47-54	8	1
β-strand	60-67	8	1
β-strand	71-75	5	1
α-helix	77-79	3
β-strand	82-85	4	1
α-helix	87-89	3
β-strand	91-92	2	1
β-strand	101-105	5	1
β-strand	112-117	6	1
β-strand	123-130	8	1
β-strand	133-140	8	1
α-helix	147-149	3
β-strand	151-154	4	1

Chain B: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	2-13	12	2
α-helix	18	1
β-strand	19-22	4	2
β-strand	28-31	4	2
α-helix	35-40	6
α-helix	42-45	4
β-strand	47-54	8	2
β-strand	60-67	8	2
β-strand	71-75	5	2
α-helix	77-79	3
β-strand	82-85	4	2
α-helix	87-89	3
β-strand	91-92	2	2
β-strand	101-105	5	2
α-helix	106	1
β-strand	112-117	6	2
β-strand	123-130	8	2
β-strand	133-140	8	2
α-helix	147-149	3
β-strand	151-154	4	2

Chain C: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	2-13	12	3
α-helix	18	1
β-strand	19-22	4	3
β-strand	28-31	4	3
α-helix	35-40	6
α-helix	42-45	4
β-strand	47-54	8	3
β-strand	60-67	8	3
β-strand	71-75	5	3
α-helix	77-79	3
β-strand	82-85	4	3
α-helix	87-89	3
β-strand	91-92	2	3
β-strand	101-105	5	3
α-helix	106	1
β-strand	113-117	5	3
β-strand	123-130	8	3
β-strand	133-140	8	3
α-helix	147-149	3
β-strand	151-154	4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interleukin-18	A, B, C, D	protein	157	Homo sapiens	Q14116 (AlphaFold model)

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

>3WO2_1 Interleukin-18 (chains A, B, C, D)
YFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQPRGM
AVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSSY
EGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED

Ligands and cofactors

ID	Name	Formula	Copies
CPS	3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate	C32 H58 N2 O7 S	12

Water and common crystallization additives (SO4) are not listed.

Primary citation

The structural basis for receptor recognition of human interleukin-18. Tsutsumi, N., Kimura, T., Arita, K. et al. Nat Commun (2014) 5:5340-5340. DOI 10.1038/ncomms6340 · PubMed

Other PDB entries of the same protein (UniProt Q14116 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2VXT 1.49 Å, Crystal structure of human IL-18 complexed to murine reference antibody 125-2H Fab
9OD9 1.6 Å, Structure of disulfide-stabilized IL-18 variant
4EKX 1.75 Å, Crystal Structure of YLDV 14L IL-18 Binding Protein in Complex with Human IL-18
7AL7 1.8 Å, The Crystal Structure of Human IL-18 in Complex With Human IL-18 Binding Protein
9OD7 1.9 Å, Structure of disulfide-stabilized IL-18 variant
4XFS 1.91 Å, Structure of IL-18 SER Mutant I
3F62 2.0 Å, Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein
4XFT 2.0 Å, Structure of IL-18 SER Mutant III
4HJJ 2.1 Å, Structure Reveals Function of the Dual Variable Domain Immunoglobulin (DVD-Ig) Molecule
4EEE 2.71 Å, Crystal Structure of YLDV 14L IL-18 Binding Protein in Complex with Human IL-18
4R6U 2.8 Å, IL-18 receptor complex
4XFU 2.85 Å, Structure of IL-18 SER Mutant V

Browse structure collections

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