Crystal Structure of the Liprin-alpha/CASK complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 12 Oct 2011.
Explore 3TAC in 3D Show helices and sheets RCSB PDB PDBe
3TAC contains 52 α-helices and 15 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 |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| α-helix | 8-11 | 4 | |
| β-strand | 12-20 | 9 | 1 |
| β-strand | 24-31 | 8 | 1 |
| β-strand | 37-44 | 8 | 1 |
| α-helix | 45-49 | 5 | |
| α-helix | 56-68 | 13 | |
| β-strand | 74 | 1 | 2 |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 86-92 | 7 | 1 |
| α-helix | 93-94 | 2 | |
| β-strand | 98 | 1 | 2 |
| α-helix | 99-108 | 10 | |
| β-strand | 111 | 1 | 3 |
| α-helix | 115-134 | 20 | |
| β-strand | 137-138 | 2 | 4 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 2 |
| α-helix | 156-157 | 2 | |
| β-strand | 158-160 | 3 | 2 |
| α-helix | 163-165 | 3 | |
| β-strand | 167-168 | 2 | 4 |
| α-helix | 169-170 | 2 | |
| β-strand | 175 | 1 | 5 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196 | 1 | 5 |
| α-helix | 199-214 | 16 | |
| α-helix | 223-232 | 10 | |
| α-helix | 239-242 | 4 | |
| α-helix | 247-256 | 10 | |
| α-helix | 265-266 | 2 | |
| α-helix | 267-271 | 5 | |
| α-helix | 274-277 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-300 | 12 | |
| α-helix | 307-311 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 874-890 | 17 | |
| α-helix | 895-897 | 3 | |
| α-helix | 900-905 | 6 | |
| α-helix | 906-910 | 5 | |
| α-helix | 915-924 | 10 | |
| α-helix | 928-932 | 5 | |
| α-helix | 936-938 | 3 | |
| α-helix | 939-943 | 5 | |
| α-helix | 948-964 | 17 | |
| α-helix | 966-969 | 4 | |
| α-helix | 971-973 | 3 | |
| β-strand | 983 | 1 | 3 |
| α-helix | 984-994 | 11 | |
| α-helix | 1021-1023 | 3 | |
| α-helix | 1024-1028 | 5 | |
| α-helix | 1029-1031 | 3 | |
| α-helix | 1035-1037 | 3 | |
| α-helix | 1038-1043 | 6 | |
| α-helix | 1048-1051 | 4 | |
| α-helix | 1056-1057 | 2 | |
| α-helix | 1058-1062 | 5 | |
| α-helix | 1068-1083 | 16 | |
| α-helix | 1088-1097 | 10 | |
| α-helix | 1105-1107 | 3 | |
| α-helix | 1110-1119 | 10 | |
| α-helix | 1123-1126 | 4 | |
| α-helix | 1127-1129 | 3 | |
| α-helix | 1136-1141 | 6 | |
| α-helix | 1147-1153 | 7 | |
| α-helix | 1161-1178 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peripheral plasma membrane protein CASK | A | protein | 361 | Homo sapiens | O14936 (AlphaFold model) |
| Liprin-alpha-2 | B | protein | 334 | Homo sapiens | O75334 (AlphaFold model) |
>3TAC_1 Peripheral plasma membrane protein CASK (chains A) MHHHHHHSSGLVPRGSMADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVD VAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIV KRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG VAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE RLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAY KIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAE R
>3TAC_2 Liprin-alpha-2 (chains B) GPGSEFGKLGTQAEKDRRLKKKHELLEEARRKGLPFAQWDGPTVVAWLELWLGMPAWYVA ACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPPTSRTPSGN VWVTHEEMENLAAQAKTKESEEGSWAQCPVFLQTLAYGDMNHEWIGNEWLPSLGLPQYRS YFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELERRREASQ HEIKDVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQ NTQARQILEREYNNLLALGTERRLDESDDKNFRR
Liprin-mediated large signaling complex organization revealed by the liprin-alpha/CASK and liprin-alpha/liprin-beta complex structures. Wei, Z., Zheng, S., Spangler, S.A. et al. Mol Cell (2011) 43:586-598. DOI 10.1016/j.molcel.2011.07.021 · PubMed
Other PDB entries of the same protein (UniProt O14936 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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