Crystal Structure of a Nucleoporin. Determined by X-ray diffraction at 2.4 Å resolution. Released 25 Sept 2013.
Explore 4MHC in 3D Show helices and sheets RCSB PDB PDBe
4MHC contains 32 α-helices and 38 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 | 90-106 | 17 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-116 | 3 | |
| β-strand | 122-126 | 5 | 1 |
| α-helix | 133-135 | 3 | |
| β-strand | 138-145 | 8 | 2 |
| α-helix | 146-147 | 2 | |
| α-helix | 148-151 | 4 | |
| β-strand | 161-166 | 6 | 3 |
| β-strand | 171-176 | 6 | 3 |
| β-strand | 179-184 | 6 | 3 |
| β-strand | 191-194 | 4 | 3 |
| β-strand | 201-207 | 7 | 4 |
| α-helix | 208-210 | 3 | |
| β-strand | 220-226 | 7 | 4 |
| β-strand | 229-237 | 9 | 4 |
| α-helix | 243 | 1 | |
| β-strand | 244-254 | 11 | 4 |
| β-strand | 260-266 | 7 | 5 |
| β-strand | 271-276 | 6 | 5 |
| β-strand | 284-286 | 3 | 5 |
| β-strand | 303-305 | 3 | 5 |
| β-strand | 342-348 | 7 | 6 |
| β-strand | 353-358 | 6 | 6 |
| β-strand | 363-369 | 7 | 6 |
| β-strand | 372-379 | 8 | 6 |
| α-helix | 381-391 | 11 | |
| α-helix | 397-399 | 3 | |
| β-strand | 406-411 | 6 | 7 |
| β-strand | 420-426 | 7 | 7 |
| β-strand | 431-435 | 5 | 7 |
| β-strand | 438-439 | 2 | 8 |
| β-strand | 442-443 | 2 | 8 |
| α-helix | 444-446 | 3 | |
| β-strand | 447-452 | 6 | 7 |
| α-helix | 453-455 | 3 | |
| α-helix | 483-486 | 4 | |
| β-strand | 495 | 1 | 1 |
| β-strand | 500-502 | 3 | 1 |
| β-strand | 506-512 | 7 | 1 |
| β-strand | 536-543 | 8 | 1 |
| α-helix | 545-551 | 7 | |
| β-strand | 555-560 | 6 | 1 |
| α-helix | 566 | 1 | |
| β-strand | 567-572 | 6 | 2 |
| α-helix | 589-592 | 4 | |
| α-helix | 597-599 | 3 | |
| β-strand | 600-605 | 6 | 2 |
| β-strand | 608-614 | 7 | 2 |
| α-helix | 615-616 | 2 | |
| α-helix | 617-623 | 7 | |
| α-helix | 629-635 | 7 | |
| α-helix | 637-649 | 13 | |
| α-helix | 655-667 | 13 | |
| β-strand | 669 | 1 | 9 |
| β-strand | 673 | 1 | 9 |
| α-helix | 707-719 | 13 | |
| β-strand | 727 | 1 | 10 |
| β-strand | 729 | 1 | 11 |
| β-strand | 745 | 1 | 11 |
| α-helix | 749-768 | 20 | |
| α-helix | 770-772 | 3 | |
| α-helix | 787-815 | 29 | |
| α-helix | 816-818 | 3 | |
| α-helix | 819-829 | 11 | |
| α-helix | 838-845 | 8 | |
| β-strand | 848 | 1 | 10 |
| α-helix | 849-853 | 5 | |
| α-helix | 857-872 | 16 | |
| α-helix | 879-890 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoporin NUP157 | A | protein | 826 | Saccharomyces cerevisiae | P40064 (AlphaFold model) |
>4MHC_1 Nucleoporin NUP157 (chains A) SMESELRDVTTHVKISGLTSSEPLQLASEFVQDLSFRDRNTPILDNPDYYSKGLDYNFSD EVGGLGAFTPFQRQQVTNIPDEVLSQVSNTEIKSDMGIFLELNYCWITSDNKLILWNINN SSEYHCIDEIEHTILKVKLVKPSPNTFVSSVENLLIVATLFDIYILTISFNDRTHELNIF NTGLKVNVTGFNVSNIISYERTGQIFFTGATDGVNVWELQYNCSENLFNSKSNKICLTKS NLANLLPTKLIPSIPGGKLIQKVLEGDAGTEEETISQLEVDQSRGVLHTLSTKSIVRSYL ITSNGLVGPVLIDAAHIRRGMNALGVKNSPLLSNRAFKIAKIVSISMCENNDLFLAVITT TGVRLYFKGSISRRSIGSLKLDSVKFPPTSISSSLEQNKSFIIGHHPLNTHDTGPLSTQK ASSTYINTTCASTIISPGIYFTCVRKRANSGELSKGITNKALLENKEEHKLYVSAPDYGI LKNYGKYVENTALLDTTDEIKEIVPLTRSFNYTSTPQGYANVFASQYSAEPLKVAVLTSN ALEIYCYRTPDEVFESLIENPLPFIHSYGLSEACSTALYLACKFNKSEHIKSSALAFFSA GIPGVVEIKPKSSRESGSVPPISQNLFDKSGECDGIVLSPRFYGSALLITRLFSQIWEER VFVFKRASKTEKMDAFGISITRPQVEYYLSSISVLADFFNIHRPSFVSFVPPKGSNAITA SDAESIAMNALILLINSIKDALSLINVFYEDIDAFKSLLNTLMGAGGVYDSKTREYFFDL KFHDLFTPNAKTKQLIKEILIEVVNANIASGTSADYIVNVLKERFG
Structure and nucleic acid binding activity of the nucleoporin Nup157. Seo, H.S., Blus, B.J., Jankovic, N.Z. et al. Proc Natl Acad Sci U S A (2013) 110:16450-16455. DOI 10.1073/pnas.1316607110 · PubMed
Other PDB entries of the same protein (UniProt P40064 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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