3F62: Human IL-18

Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Jan 2009.

Method
X-ray diffraction
Resolution
2.0 Å
Organisms
Ectromelia virus, Homo sapiens
Chains
2
Atoms
2,146
Mol. weight
30.6 kDa
Released
6 Jan 2009

Explore 3F62 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3F62 contains 9 α-helices and 22 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: 4 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix22-243
β-strand29-3351
β-strand36-4381
β-strand51-5882
α-helix63-653
β-strand66-6722
α-helix68-703
β-strand75-7731
α-helix78-803
β-strand81-8551
β-strand88-97101
β-strand106-11492
β-strand117-12372
Chain B: 5 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand2-13123
α-helix181
β-strand19-2243
β-strand28-3143
α-helix43-453
β-strand47-5483
β-strand60-6783
β-strand71-7553
α-helix77-793
β-strand82-8543
α-helix87-893
β-strand91-9223
β-strand101-10663
β-strand109-11793
β-strand123-12863
β-strand135-14063
α-helix147-1493
β-strand151-15553

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interleukin 18 binding proteinAprotein109Ectromelia virusQ85319
Interleukin-18Bprotein158Homo sapiensQ14116 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3F62_1 Interleukin 18 binding protein (chains A)
GAMVETKCPNLDIVTSSGEFHCSGCVEHMPEFSYMYWLAKDMKSDEDTKFIEHLGDGINE
DETVRTTDGGITTLRKVLHVTDTNKFAHYRFTCVLTTLDGVSKKNIWLK
Sequence of entity 2 (B), FASTA
>3F62_2 Interleukin-18 (chains B)
GYFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDSRDNAPRTIFIISMYKDSQPRG
MAVTISVKSEKISTLSSENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSS
YEGYFLASEKERDLFKLILKKEDELGDRSIMFTVQNED

Primary citation

Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein. Krumm, B., Meng, X., Li, Y. et al. Proc Natl Acad Sci U S A (2008) 105:20711-20715. DOI 10.1073/pnas.0809086106 · PubMed

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