The structure of the KANK2 ankyrin domain with the KIF21A peptide. Determined by X-ray diffraction at 2.12 Å resolution. Released 6 Dec 2017.
Explore 5YBV in 3D Show helices and sheets RCSB PDB PDBe
5YBV contains 36 α-helices and 0 β-strands across 4 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 | 592-606 | 15 | |
| α-helix | 608-610 | 3 | |
| α-helix | 613-631 | 19 | |
| α-helix | 638-651 | 14 | |
| α-helix | 653-660 | 8 | |
| α-helix | 670-676 | 7 | |
| α-helix | 680-688 | 9 | |
| α-helix | 704-707 | 4 | |
| α-helix | 708-710 | 3 | |
| α-helix | 716-727 | 12 | |
| α-helix | 742-748 | 7 | |
| α-helix | 752-760 | 9 | |
| α-helix | 775-782 | 8 | |
| α-helix | 785-792 | 8 | |
| α-helix | 809-815 | 7 | |
| α-helix | 819-828 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 592-606 | 15 | |
| α-helix | 608-610 | 3 | |
| α-helix | 613-631 | 19 | |
| α-helix | 638-649 | 12 | |
| α-helix | 653-660 | 8 | |
| α-helix | 670-676 | 7 | |
| α-helix | 680-688 | 9 | |
| α-helix | 704-707 | 4 | |
| α-helix | 708-710 | 3 | |
| α-helix | 716-728 | 13 | |
| α-helix | 742-748 | 7 | |
| α-helix | 752-760 | 9 | |
| α-helix | 775-782 | 8 | |
| α-helix | 785-792 | 8 | |
| α-helix | 809-815 | 7 | |
| α-helix | 819-828 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1153-1155 | 3 | |
| α-helix | 1160-1164 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| KN motif and ankyrin repeat domain-containing protein 2 | A | protein | 258 | Homo sapiens | Q63ZY3 (AlphaFold model) |
| KN motif and ankyrin repeat domain-containing protein 2 | B | protein | 261 | Homo sapiens | Q63ZY3 (AlphaFold model) |
| Kinesin-like protein KIF21A | C, D | protein | 22 | Homo sapiens | Q7Z4S6 (AlphaFold model) |
>5YBV_1 KN motif and ankyrin repeat domain-containing protein 2 (chains A) GHMSGSNTEEEIRMELSPDLISACLALEKYLDNPNALTERELKVAYTTVLQEWLRLACRS DAHPELVRRHLVTFRAMSARLLDYVVNIADSNGNTALHYSVSHANFPVVQQLLDSGVCKV DKQNRAGYSPIMLTALATLKTQDDIETVLQLFRLGNINAKASQAGQTALMLAVSHGRVDV VKALLACEADVNVQDDDGSTALMCACEHGHKEIAGLLLAVPSCDISLTDRDGSTALMVAL DAGQSEIASMLYSRMNIK
>5YBV_2 KN motif and ankyrin repeat domain-containing protein 2 (chains B) GHMGHMSGSNTEEEIRMELSPDLISACLALEKYLDNPNALTERELKVAYTTVLQEWLRLA CRSDAHPELVRRHLVTFRAMSARLLDYVVNIADSNGNTALHYSVSHANFPVVQQLLDSGV CKVDKQNRAGYSPIMLTALATLKTQDDIETVLQLFRLGNINAKASQAGQTALMLAVSHGR VDVVKALLACEADVNVQDDDGSTALMCACEHGHKEIAGLLLAVPSCDISLTDRDGSTALM VALDAGQSEIASMLYSRMNIK
>5YBV_3 Kinesin-like protein KIF21A (chains C, D) EVKPKNKARRRTTTQMELLYAD
Structural basis for the recognition of kinesin family member 21A (KIF21A) by the ankyrin domains of KANK1 and KANK2 proteins. Guo, Q., Liao, S., Zhu, Z. et al. J Biol Chem (2018) 293:557-566. DOI 10.1074/jbc.M117.817494 · PubMed
Other PDB entries of the same protein (UniProt Q63ZY3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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