Overall structure of Patj/Pals1/Mals complex. Determined by X-ray diffraction at 2.05 Å resolution. Released 22 Feb 2012.
Explore 3UIT in 3D Show helices and sheets RCSB PDB PDBe
3UIT contains 66 α-helices and 8 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 | 11-26 | 16 | |
| α-helix | 32-43 | 12 | |
| α-helix | 45-56 | 12 | |
| β-strand | 60 | 1 | 1 |
| α-helix | 69-71 | 3 | |
| α-helix | 82-95 | 14 | |
| α-helix | 99-113 | 15 | |
| α-helix | 115-131 | 17 | |
| α-helix | 136-137 | 2 | |
| α-helix | 144-155 | 12 | |
| α-helix | 161-171 | 11 | |
| α-helix | 173-187 | 15 | |
| α-helix | 194-198 | 5 | |
| α-helix | 200-202 | 3 | |
| α-helix | 206-226 | 21 | |
| α-helix | 232-242 | 11 | |
| α-helix | 244-258 | 15 | |
| β-strand | 260 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-26 | 16 | |
| α-helix | 32-43 | 12 | |
| α-helix | 45-56 | 12 | |
| β-strand | 60 | 1 | 3 |
| α-helix | 69-71 | 3 | |
| α-helix | 82-95 | 14 | |
| α-helix | 99-113 | 15 | |
| α-helix | 115-131 | 17 | |
| α-helix | 136-137 | 2 | |
| α-helix | 144-155 | 12 | |
| α-helix | 156-158 | 3 | |
| α-helix | 161-171 | 11 | |
| α-helix | 173-186 | 14 | |
| α-helix | 194-198 | 5 | |
| α-helix | 200-202 | 3 | |
| α-helix | 206-226 | 21 | |
| α-helix | 232-242 | 11 | |
| α-helix | 244-258 | 15 | |
| β-strand | 260 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-26 | 17 | |
| α-helix | 32-43 | 12 | |
| α-helix | 45-56 | 12 | |
| β-strand | 60 | 1 | 4 |
| α-helix | 69-71 | 3 | |
| α-helix | 82-93 | 12 | |
| α-helix | 99-113 | 15 | |
| α-helix | 115-131 | 17 | |
| α-helix | 136-137 | 2 | |
| α-helix | 144-155 | 12 | |
| α-helix | 163-169 | 7 | |
| α-helix | 173-186 | 14 | |
| α-helix | 194-198 | 5 | |
| α-helix | 200-202 | 3 | |
| α-helix | 206-226 | 21 | |
| α-helix | 232-242 | 11 | |
| α-helix | 244-258 | 15 | |
| β-strand | 260 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-25 | 15 | |
| α-helix | 32-43 | 12 | |
| α-helix | 45-56 | 12 | |
| β-strand | 60 | 1 | 2 |
| α-helix | 64-66 | 3 | |
| α-helix | 69-71 | 3 | |
| α-helix | 82-95 | 14 | |
| α-helix | 99-113 | 15 | |
| α-helix | 115-131 | 17 | |
| α-helix | 136-137 | 2 | |
| α-helix | 144-155 | 12 | |
| α-helix | 162-171 | 10 | |
| α-helix | 173-186 | 14 | |
| α-helix | 194-198 | 5 | |
| α-helix | 200-202 | 3 | |
| α-helix | 206-225 | 20 | |
| α-helix | 232-242 | 11 | |
| α-helix | 244-259 | 16 | |
| β-strand | 260 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| InaD-like protein, MAGUK p55 subfamily member 5, Protein lin-7 homolog B | A, B, C, D | protein | 265 | Mus musculus, Rattus norvegicus, Homo sapiens | F1MAD2 (AlphaFold model), O88951 (AlphaFold model), Q8N3R9 (AlphaFold model) |
>3UIT_1 InaD-like protein, MAGUK p55 subfamily member 5, Protein lin-7 homolog B (chains A, B, C, D) MPENPAAEKMQVLQVLDRLRGKLQEKGDTTQNEKLSAFYETLKSPLFNQILTLQQSIKQL KGQLSHIPLEVLFQGPVKILEIEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNKDFQNA FKIHNAITVHMNKASPPFPLISNAQDLAQEVQTVLKPVHHKEGQELTALLNTPHIQALLL AHDKVAEQEMGGGLEVLFQGPALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRV LQSRFCSAIREVYEQLYDTLDITGS
Structure of an L27 domain heterotrimer from cell polarity complex Patj/Pals1/Mals2 reveals mutually independent L27 domain assembly mode. Zhang, J., Yang, X., Wang, Z. et al. J Biol Chem (2012) 287:11132-11140. DOI 10.1074/jbc.M111.321216 · PubMed
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