Cryo-EM structure of KIFBP:KIF15. Determined by electron microscopy at 4.8 Å resolution. Released 8 Sept 2021.
Explore 7RYP in 3D Show helices and sheets RCSB PDB PDBe
7RYP contains 33 α-helices and 23 β-strands across 2 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 | 28-33 | 6 | 1 |
| α-helix | 36-38 | 3 | |
| β-strand | 58-60 | 3 | 2 |
| β-strand | 69-71 | 3 | 2 |
| β-strand | 74-76 | 3 | 1 |
| α-helix | 82-85 | 4 | |
| α-helix | 86-90 | 5 | |
| α-helix | 91-99 | 9 | |
| β-strand | 101 | 1 | 3 |
| β-strand | 103-105 | 3 | 4 |
| β-strand | 106 | 1 | 1 |
| α-helix | 116-119 | 4 | |
| β-strand | 123 | 1 | 5 |
| β-strand | 125 | 1 | 5 |
| α-helix | 131-133 | 3 | |
| α-helix | 135-153 | 19 | |
| β-strand | 158-160 | 3 | 4 |
| β-strand | 162-170 | 9 | 4 |
| β-strand | 173-176 | 4 | 4 |
| β-strand | 186-187 | 2 | 6 |
| β-strand | 193 | 1 | 7 |
| β-strand | 197-198 | 2 | 6 |
| β-strand | 203-205 | 3 | 4 |
| α-helix | 208-220 | 13 | |
| β-strand | 237-248 | 12 | 4 |
| β-strand | 256-264 | 9 | 4 |
| α-helix | 271-273 | 3 | |
| α-helix | 276-290 | 15 | |
| α-helix | 319-325 | 7 | |
| β-strand | 333 | 1 | 4 |
| β-strand | 335-340 | 6 | 1 |
| α-helix | 344-346 | 3 | |
| α-helix | 347-360 | 14 | |
| β-strand | 369 | 1 | 3 |
| β-strand | 371 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-21 | 16 | |
| α-helix | 39-50 | 12 | |
| α-helix | 87-104 | 18 | |
| α-helix | 112-126 | 15 | |
| α-helix | 137-151 | 15 | |
| α-helix | 155-172 | 18 | |
| α-helix | 202-221 | 20 | |
| α-helix | 224-240 | 17 | |
| α-helix | 246-262 | 17 | |
| α-helix | 266-279 | 14 | |
| α-helix | 302-325 | 24 | |
| α-helix | 330-332 | 3 | |
| α-helix | 347-360 | 14 | |
| α-helix | 361-363 | 3 | |
| α-helix | 369-381 | 13 | |
| α-helix | 390-409 | 20 | |
| α-helix | 415-433 | 19 | |
| α-helix | 441-454 | 14 | |
| α-helix | 455-458 | 4 | |
| β-strand | 460 | 1 | 7 |
| α-helix | 465-485 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin-like protein KIF15 | A | protein | 375 | Homo sapiens | Q9NS87 (AlphaFold model) |
| KIF-binding protein | B | protein | 621 | Homo sapiens | Q96EK5 (AlphaFold model) |
>7RYP_1 Kinesin-like protein KIF15 (chains A) MAPGCKTELRSVTNGQSNQPSNEGDAIKVFVRIRPPAERSGSADGEQNLCLSVLSSTSLR LHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIFAYGQTGSGKTFTMM GPSESDNFSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEIYNEQIYDLLDS ASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVF TITIESMEKSNEIVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVIT ALVDVGNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRA KLIKNKAVVNEDTQG
>7RYP_2 KIF-binding protein (chains B) MANVPWAEVCEKFQAALALSRVELHKNPEKEPYKSKYSARALLEEVKALLGPAPEDEDER PEAEDGPGAGDHALGLPAEVVEPEGPVAQRAVRLAVIEFHLGVNHIDTEELSAGEEHLVK CLRLLRRYRLSHDCISLCIQAQNNLGILWSEREEIETAQAYLESSEALYNQYMKEVGSPP LDPTERFLPEEEKLTEQERSKRFEKVYTHNLYYLAQVYQHLEMFEKAAHYCHSTLKRQLE HNAYHPIEWAINAATLSQFYINKLCFMEARHCLSAANVIFGQTGKISATEDTPEAEGEVP ELYHQRKGEIARCWIKYCLTLMQNAQLSMQDNIGELDLDKQSELRALRKKELDEEESIRK KAVQFGTGELCDAISAVEEKVSYLRPLDFEEARELFLLGQHYVFEAKEFFQIDGYVTDHI EVVQDHSALFKVLAFFETDMERRCKMHKRRIAMLEPLTVDLNPQYYLLVNRQIQFEIAHA YYDMMDLKVAIADRLRDPDSHIVKKINNLNKSALKYYQLFLDSLRDPNKVFPEHIGEDVL RPAMLAKFRVARLYGKIITADPKKELENLATSLEHYKFIVDYCEKHPEAAQEIEVELELS KEMVSLLPTKMERFRTKMALT
Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding. Solon, A.L., Tan, Z., Schutt, K.L. et al. Sci Adv (2021) 7:eabj9812-eabj9812. DOI 10.1126/sciadv.abj9812 · PubMed
Other PDB entries of the same protein (UniProt Q9NS87 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7RYP directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.