Structure of importin-alpha: dUTPase NLS complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Nov 2013.
Explore 4MZ5 in 3D Show helices and sheets RCSB PDB PDBe
4MZ5 contains 33 α-helices and 0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 78-85 | 8 | |
| α-helix | 90-104 | 15 | |
| α-helix | 112-117 | 6 | |
| α-helix | 121-127 | 7 | |
| α-helix | 134-148 | 15 | |
| α-helix | 152-160 | 9 | |
| α-helix | 163-170 | 8 | |
| α-helix | 176-190 | 15 | |
| α-helix | 194-202 | 9 | |
| α-helix | 206-212 | 7 | |
| α-helix | 218-220 | 3 | |
| α-helix | 223-236 | 14 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-259 | 14 | |
| α-helix | 265-278 | 14 | |
| α-helix | 283-290 | 8 | |
| α-helix | 295-302 | 8 | |
| α-helix | 307-320 | 14 | |
| α-helix | 325-333 | 9 | |
| α-helix | 336-338 | 3 | |
| α-helix | 340-343 | 4 | |
| α-helix | 349-362 | 14 | |
| α-helix | 367-375 | 9 | |
| α-helix | 378-387 | 10 | |
| α-helix | 391-407 | 17 | |
| α-helix | 410-418 | 9 | |
| α-helix | 422-427 | 6 | |
| α-helix | 428-430 | 3 | |
| α-helix | 434-452 | 19 | |
| α-helix | 457-466 | 10 | |
| α-helix | 469-475 | 7 | |
| α-helix | 476-478 | 3 | |
| α-helix | 482-495 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial | A, C | protein | 13 | Homo sapiens | P33316 (AlphaFold model) |
| Importin subunit alpha-1 | E | protein | 509 | Mus musculus | P52293 (AlphaFold model) |
>4MZ5_1 Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (chains A, C) AISPSKRARPAEV
>4MZ5_2 Importin subunit alpha-1 (chains E) MHHHHHHSSGLVPRGSGMLETAAALFERNHMDSPDLGTDDDDLAMADIGSNQGTVNWSVE DIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFE SAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSAFRDL VIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRL LHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGN IVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLV PFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQV ILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASLNLIEKYFSVE EEEDQNVVPETTSEGFAFQVQDGAPGTFN
Phosphorylation adjacent to the nuclear localization signal of human dUTPase abolishes nuclear import: structural and mechanistic insights. Rona, G., Marfori, M., Borsos, M. et al. Acta Crystallogr D Biol Crystallogr (2013) 69:2495-2505. DOI 10.1107/S0907444913023354 · PubMed
Other PDB entries of the same protein (UniProt P33316 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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