Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1. Determined by X-ray diffraction at 1.65 Å resolution. Released 2 Jun 2010.
Explore 3MMY in 3D Show helices and sheets RCSB PDB PDBe
3MMY contains 52 α-helices and 140 β-strands across 8 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 |
|---|---|---|---|
| β-strand | 12 | 1 | 1 |
| β-strand | 15-16 | 2 | 2 |
| α-helix | 31 | 1 | |
| β-strand | 32-33 | 2 | 3 |
| α-helix | 34 | 1 | |
| β-strand | 42-47 | 6 | 4 |
| α-helix | 48-49 | 2 | |
| β-strand | 55-61 | 7 | 4 |
| β-strand | 65-71 | 7 | 4 |
| β-strand | 77-84 | 8 | 4 |
| β-strand | 89-94 | 6 | 5 |
| β-strand | 100-105 | 6 | 5 |
| β-strand | 109-114 | 6 | 5 |
| β-strand | 119-125 | 7 | 5 |
| β-strand | 130-137 | 8 | 6 |
| β-strand | 142-148 | 7 | 6 |
| β-strand | 152-156 | 5 | 6 |
| β-strand | 165-168 | 4 | 6 |
| β-strand | 173-179 | 7 | 7 |
| β-strand | 182-187 | 6 | 7 |
| α-helix | 188-190 | 3 | |
| β-strand | 192-196 | 5 | 7 |
| β-strand | 202-206 | 5 | 7 |
| β-strand | 215-222 | 8 | 8 |
| β-strand | 228-235 | 8 | 8 |
| β-strand | 239-244 | 6 | 8 |
| α-helix | 250-253 | 4 | |
| β-strand | 255-258 | 4 | 8 |
| β-strand | 261-262 | 2 | 9 |
| α-helix | 269-270 | 2 | |
| β-strand | 271-273 | 3 | 9 |
| β-strand | 276-281 | 6 | 10 |
| β-strand | 288-292 | 5 | 10 |
| β-strand | 297-301 | 5 | 10 |
| β-strand | 306-310 | 5 | 10 |
| α-helix | 311-314 | 4 | |
| β-strand | 318-323 | 6 | 3 |
| β-strand | 330-334 | 5 | 3 |
| α-helix | 342-344 | 3 | |
| α-helix | 350-351 | 2 | |
| β-strand | 352-356 | 5 | 3 |
| β-strand | 364 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 163-164 | 2 | |
| α-helix | 166-167 | 2 | |
| β-strand | 168-172 | 5 | 9 |
| β-strand | 181-186 | 6 | 9 |
| α-helix | 189-191 | 3 | |
| α-helix | 200-209 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12 | 1 | 11 |
| β-strand | 15-16 | 2 | 10 |
| α-helix | 31 | 1 | |
| β-strand | 32-33 | 2 | 12 |
| α-helix | 34 | 1 | |
| β-strand | 42-47 | 6 | 13 |
| α-helix | 48-49 | 2 | |
| β-strand | 55-61 | 7 | 13 |
| β-strand | 65-71 | 7 | 13 |
| β-strand | 77-84 | 8 | 13 |
| β-strand | 89-94 | 6 | 14 |
| β-strand | 100-105 | 6 | 14 |
| β-strand | 109-114 | 6 | 14 |
| β-strand | 119-125 | 7 | 14 |
| β-strand | 130-137 | 8 | 15 |
| β-strand | 142-148 | 7 | 15 |
| β-strand | 152-156 | 5 | 15 |
| β-strand | 165-168 | 4 | 15 |
| β-strand | 173-179 | 7 | 16 |
| β-strand | 182-187 | 6 | 16 |
| α-helix | 188-190 | 3 | |
| β-strand | 191-196 | 6 | 16 |
| β-strand | 202-206 | 5 | 16 |
| β-strand | 215-222 | 8 | 17 |
| β-strand | 228-235 | 8 | 17 |
| β-strand | 239-244 | 6 | 17 |
| α-helix | 250-253 | 4 | |
| β-strand | 255-258 | 4 | 17 |
| β-strand | 261 | 1 | 18 |
| α-helix | 270 | 1 | |
| β-strand | 271-273 | 3 | 18 |
| β-strand | 276-281 | 6 | 2 |
| β-strand | 288-292 | 5 | 2 |
| β-strand | 297-301 | 5 | 2 |
| β-strand | 306-310 | 5 | 2 |
| α-helix | 311-314 | 4 | |
| β-strand | 318-323 | 6 | 12 |
| β-strand | 330-334 | 5 | 12 |
| α-helix | 342-344 | 3 | |
| α-helix | 350-351 | 2 | |
| β-strand | 352-356 | 5 | 12 |
| β-strand | 364 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| mRNA export factor | A, C, E, G | protein | 368 | Homo sapiens | P78406 (AlphaFold model) |
| Nuclear pore complex protein Nup98 | B, D, F, H | protein | 56 | Homo sapiens | P52948 (AlphaFold model) |
>3MMY_1 mRNA export factor (chains A, C, E, G) MSLFGTTSGFGTSGTSMFGSATTDNHNPMKDIEVTSSPDDSIGCLSFSPPTLPGNFLIAG SWANDVRCWEVQDSGQTIPKAQQMHTGPVLDVCWSDDGSKVFTASCDKTAKMWDLSSNQA IQIAQHDAPVKTIHWIKAPNYSCVMTGSWDKTLKFWDTRSSNPMMVLQLPERCYCADVIY PMAVVATAERGLIVYQLENQPSEFRRIESPLKHQHRCVAIFKDKQNKPTGFALGSIEGRV AIHYINPPNPAKDNFTFKCHRSNGTNTSAPQDIYAVNGIAFHPVHGTLATVGSDGRFSFW DKDARTKLKTSEQLDQPISACCFNHNGNIFAYASSYDWSKGHEFYNPQKKNYIFLRNAAE ELKPRNKK
>3MMY_2 Nuclear pore complex protein Nup98 (chains B, D, F, H) TGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRK
Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1. Ren, Y., Seo, H.S., Blobel, G. et al. Proc Natl Acad Sci U S A (2010) 107:10406-10411. DOI 10.1073/pnas.1005389107 · PubMed
Other PDB entries of the same protein (UniProt P78406 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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