5IEC: Therapeutic inhibition of complement C5

Structural basis for therapeutic inhibition of complement C5. Determined by solution NMR. Released 27 Apr 2016.

Method: Solution NMR
Organism: Rhipicephalus appendiculatus
Chains: 1
Atoms: 515
Mol. weight: 7.48 kDa
Released: 27 Apr 2016

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

Secondary structure: helices and β-sheets

5IEC contains 2 α-helices and 4 β-strands across 1 chain. 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: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	23-26	4
α-helix	30-36	7
β-strand	40-41	2	1
β-strand	59-60	2	2
β-strand	73-74	2	1
β-strand	77-78	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RaCI2	A	protein	70	Rhipicephalus appendiculatus	A0A158RFT4 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5IEC_1 RaCI2 (chains A)
GPMEEANTTPISVKDQCANVTCRRTVDNRGKRHIDGCPPGCLCVLKGPDSKDNLDGTCYL
LATTPKSTTT

Primary citation

Structural basis for therapeutic inhibition of complement C5. Jore, M.M., Johnson, S., Sheppard, D. et al. Nat Struct Mol Biol (2016) 23:378-386. DOI 10.1038/nsmb.3196 · PubMed

Other PDB entries of the same protein (UniProt A0A158RFT4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5HCD 2.98 Å, Ternary complex of human Complement C5 with Ornithodoros moubata OmCI and Rhipicephalus…

Browse structure collections

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