The ankyrin repeat domain of Huntingtin interacting protein 14. Determined by X-ray diffraction at 1.99 Å resolution. Released 23 Jun 2009.
Explore 3EU9 in 3D Show helices and sheets RCSB PDB PDBe
3EU9 contains 44 α-helices and 12 β-strands across 3 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 | 56-58 | 3 | |
| α-helix | 61-66 | 6 | |
| α-helix | 70-78 | 9 | |
| α-helix | 93-99 | 7 | |
| α-helix | 103-111 | 9 | |
| β-strand | 120 | 1 | 1 |
| β-strand | 125 | 1 | 1 |
| α-helix | 127-134 | 8 | |
| α-helix | 137-145 | 9 | |
| α-helix | 160-166 | 7 | |
| α-helix | 170-178 | 9 | |
| α-helix | 193-200 | 8 | |
| α-helix | 207-212 | 6 | |
| α-helix | 228-235 | 8 | |
| α-helix | 238-247 | 10 | |
| β-strand | 254 | 1 | 2 |
| β-strand | 260 | 1 | 2 |
| α-helix | 261-267 | 7 | |
| α-helix | 271-280 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 56-58 | 3 | |
| α-helix | 61-66 | 6 | |
| α-helix | 70-78 | 9 | |
| α-helix | 93-99 | 7 | |
| α-helix | 103-111 | 9 | |
| β-strand | 120 | 1 | 3 |
| β-strand | 125 | 1 | 3 |
| α-helix | 127-134 | 8 | |
| α-helix | 137-144 | 8 | |
| α-helix | 160-166 | 7 | |
| α-helix | 170-179 | 10 | |
| α-helix | 193-200 | 8 | |
| α-helix | 207-212 | 6 | |
| β-strand | 220 | 1 | 4 |
| β-strand | 227 | 1 | 4 |
| α-helix | 228-234 | 7 | |
| α-helix | 238-246 | 9 | |
| α-helix | 262-268 | 7 | |
| α-helix | 271-278 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 61-66 | 6 | |
| α-helix | 70-78 | 9 | |
| α-helix | 93-99 | 7 | |
| α-helix | 103-111 | 9 | |
| β-strand | 120 | 1 | 5 |
| β-strand | 125 | 1 | 5 |
| α-helix | 127-134 | 8 | |
| α-helix | 137-145 | 9 | |
| α-helix | 160-166 | 7 | |
| α-helix | 170-178 | 9 | |
| α-helix | 193-200 | 8 | |
| α-helix | 207-212 | 6 | |
| β-strand | 220 | 1 | 6 |
| β-strand | 227 | 1 | 6 |
| α-helix | 228-234 | 7 | |
| α-helix | 238-246 | 9 | |
| α-helix | 261-268 | 8 | |
| α-helix | 271-283 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Huntingtin-interacting protein 14 | A, B, C | protein | 240 | Homo sapiens | Q8IUH5 (AlphaFold model) |
>3EU9_1 Huntingtin-interacting protein 14 (chains A, B, C) HMTHIDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKY YISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFG HTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTA LHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDN
| ID | Name | Formula | Copies |
|---|---|---|---|
| HIS | Histidine | C6 H10 N3 O2 | 1 |
Water and common crystallization additives (SO4, GOL) are not listed.
The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding. Gao, T., Collins, R.E., Horton, J.R. et al. Proteins (2009) 76:772-777. DOI 10.1002/prot.22452 · PubMed
Other PDB entries of the same protein (UniProt Q8IUH5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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