4XFU: IL-18 SER Mutant V

Structure of IL-18 SER Mutant V. Determined by X-ray diffraction at 2.85 Å resolution. Released 10 Jun 2015.

Method
X-ray diffraction
Resolution
2.85 Å
Organism
Homo sapiens
Chains
2
Atoms
2,418
Mol. weight
36.31 kDa
Released
10 Jun 2015

Explore 4XFU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4XFU contains 8 α-helices and 27 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, 13 β-strands

ElementResiduesLengthSheet
β-strand2-13121
α-helix181
β-strand19-2241
β-strand28-3141
β-strand47-5481
β-strand60-6671
β-strand73-7531
α-helix77-793
β-strand82-8431
α-helix87-893
β-strand91-9221
β-strand101-10551
β-strand112-11761
β-strand123-12971
β-strand134-14071
α-helix147-1493
β-strand151-15551
Chain B: 4 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand2-1092
β-strand1312
α-helix181
β-strand19-2242
β-strand28-3142
β-strand47-5482
β-strand60-6672
β-strand73-7532
β-strand82-8432
α-helix87-893
β-strand91-9222
β-strand101-10552
α-helix1061
β-strand113-11752
β-strand123-12972
β-strand134-14072
α-helix147-1493
β-strand151-15222

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interleukin-18A, Bprotein157Homo sapiensQ14116 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4XFU_1 Interleukin-18 (chains A, B)
YFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQRRGM
AVTISVACAAASTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRRVPGHDNKMQFESSSY
EGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED

Primary citation

Crystallization of interleukin-18 for structure-based inhibitor design. Krumm, B., Meng, X., Xiang, Y. et al. Acta Crystallogr F Struct Biol Commun (2015) 71:710-717. DOI 10.1107/S2053230X15006871 · PubMed

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

Browse structure collections

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