Structure of the Cif:Nedd8 complex - Yersinia pseudotuberculosis Cycle Inhibiting Factor in complex with human Nedd8. Determined by X-ray diffraction at 1.95 Å resolution. Released 20 Jun 2012.
Explore 4F8C in 3D Show helices and sheets RCSB PDB PDBe
4F8C contains 39 α-helices and 37 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-53 | 13 | |
| α-helix | 57-63 | 7 | |
| α-helix | 72-74 | 3 | |
| α-helix | 77-95 | 19 | |
| α-helix | 99-106 | 8 | |
| β-strand | 115 | 1 | 1 |
| α-helix | 117-129 | 13 | |
| β-strand | 131 | 1 | 2 |
| β-strand | 134 | 1 | 2 |
| α-helix | 142-143 | 2 | |
| β-strand | 144 | 1 | 3 |
| α-helix | 146-153 | 8 | |
| β-strand | 161-168 | 8 | 3 |
| β-strand | 173-179 | 7 | 3 |
| β-strand | 188-189 | 2 | 4 |
| β-strand | 190-192 | 3 | 3 |
| β-strand | 195 | 1 | 5 |
| β-strand | 204 | 1 | 5 |
| α-helix | 206-212 | 7 | |
| β-strand | 218-219 | 2 | 4 |
| α-helix | 220-229 | 10 | |
| α-helix | 237-244 | 8 | |
| α-helix | 250-252 | 3 | |
| α-helix | 255-257 | 3 | |
| α-helix | 260-262 | 3 | |
| β-strand | 266-273 | 8 | 3 |
| α-helix | 275-285 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 6 |
| β-strand | 12-16 | 5 | 6 |
| β-strand | 22 | 1 | 7 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-45 | 4 | 6 |
| β-strand | 48-49 | 2 | 6 |
| β-strand | 55 | 1 | 7 |
| α-helix | 56-59 | 4 | |
| β-strand | 66-70 | 5 | 6 |
| β-strand | 72 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-53 | 13 | |
| α-helix | 57-63 | 7 | |
| α-helix | 72-74 | 3 | |
| α-helix | 77-95 | 19 | |
| α-helix | 99-106 | 8 | |
| β-strand | 115 | 1 | 8 |
| α-helix | 117-129 | 13 | |
| α-helix | 138-140 | 3 | |
| α-helix | 142-145 | 4 | |
| α-helix | 146-155 | 10 | |
| β-strand | 161-168 | 8 | 9 |
| β-strand | 173-179 | 7 | 9 |
| β-strand | 189 | 1 | 10 |
| β-strand | 190-192 | 3 | 9 |
| β-strand | 195 | 1 | 11 |
| α-helix | 202-203 | 2 | |
| β-strand | 204 | 1 | 11 |
| α-helix | 206-212 | 7 | |
| β-strand | 218 | 1 | 10 |
| α-helix | 220-231 | 12 | |
| α-helix | 237-244 | 8 | |
| α-helix | 250-252 | 3 | |
| α-helix | 255-257 | 3 | |
| α-helix | 260-262 | 3 | |
| β-strand | 266-273 | 8 | 9 |
| α-helix | 275-285 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 12 |
| β-strand | 12-16 | 5 | 12 |
| β-strand | 22 | 1 | 13 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-45 | 4 | 12 |
| β-strand | 48-49 | 2 | 12 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 13 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-70 | 5 | 12 |
| β-strand | 72 | 1 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cycle Inhibiting Factor | A, C | protein | 275 | Yersinia pseudotuberculosis | A0A0H3B1Q8 (AlphaFold model) |
| NEDD8 | B, D | protein | 88 | Homo sapiens | Q15843 (AlphaFold model) |
>4F8C_1 Cycle Inhibiting Factor (chains A, C) MAHHHHHHSSGLEVLFQGPPVSHSINNPSIQHVQDFATLSARSLRANVLLNSDDHSVPIH AKNPSELLEAIDNNISQTAQDWGVSIQEVEVILGSSKRIIEPVAGVTANTIMKLFLDNDI FSYSFEKGQSLSLSQLQERLASLPAHKNFILRVNDGGLGHAYVIDFPATTNPSRDAFLYQ SDLGEGVTREVRFEDWMTQKASHPISLDDINTHFIGIAQDQIDLAHIAKLFDVDGNVKML RADHLISHKTSEFNFQLFEYDLKNLENNMSIIKTH
>4F8C_2 NEDD8 (chains B, D) MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYK ILGGSVLHLVLALRGGGGLRQKHHHHHH
The molecular basis of Nedd8 deamidation by the bacterial effector protein Cif. Crow, A., Hughes, R.K., Taieb, F. et al. Proc Natl Acad Sci U S A (2012).
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