9IMP: The complex of PDZ3 and PBM
The complex of PDZ3 and PBM. Determined by X-ray diffraction at 2.87 Å resolution. Released 11 Sept 2024.
- Method
- X-ray diffraction
- Resolution
- 2.87 Å
- Organisms
- Rattus norvegicus, Mus musculus
- Chains
- 12
- Atoms
- 4,605
- Mol. weight
- 78.53 kDa
- Released
- 11 Sept 2024
Explore 9IMP in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9IMP contains 18 α-helices and 42 β-strands across 12 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.
Chain A: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 584-592 | 9 | 1 |
| β-strand | 603-610 | 8 | 1 |
| β-strand | 615-624 | 10 | 1 |
| α-helix | 629-633 | 5 | |
| α-helix | 640 | 1 | |
| β-strand | 641-645 | 5 | 1 |
| β-strand | 648-649 | 2 | 1 |
| α-helix | 655-664 | 10 | |
| β-strand | 675-683 | 9 | 1 |
Chain B: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 584-592 | 9 | 2 |
| β-strand | 603-610 | 8 | 2 |
| β-strand | 615-624 | 10 | 2 |
| α-helix | 629-633 | 5 | |
| α-helix | 640 | 1 | |
| β-strand | 641-645 | 5 | 2 |
| β-strand | 648-649 | 2 | 2 |
| α-helix | 655-667 | 13 | |
| β-strand | 675-683 | 9 | 2 |
Chain C: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 584-592 | 9 | 2 |
| β-strand | 603-609 | 7 | 2 |
| β-strand | 616-624 | 9 | 2 |
| α-helix | 629-633 | 5 | |
| α-helix | 640 | 1 | |
| β-strand | 641-645 | 5 | 2 |
| β-strand | 648-649 | 2 | 2 |
| α-helix | 655-664 | 10 | |
| β-strand | 675-683 | 9 | 2 |
Chain D: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 584-592 | 9 | 1 |
| β-strand | 603-608 | 6 | 1 |
| β-strand | 618-624 | 7 | 1 |
| α-helix | 629-633 | 5 | |
| α-helix | 640 | 1 | |
| β-strand | 641-645 | 5 | 1 |
| β-strand | 648-649 | 2 | 1 |
| α-helix | 655-666 | 12 | |
| β-strand | 675-683 | 9 | 1 |
Chain E: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 584-591 | 8 | 1 |
| β-strand | 603-610 | 8 | 1 |
| β-strand | 615-624 | 10 | 1 |
| α-helix | 629-633 | 5 | |
| α-helix | 640 | 1 | |
| β-strand | 641-645 | 5 | 1 |
| β-strand | 648-649 | 2 | 1 |
| α-helix | 655-667 | 13 | |
| β-strand | 676-683 | 8 | 1 |
Chain F: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 584-591 | 8 | 2 |
| β-strand | 603-607 | 5 | 2 |
| β-strand | 619-624 | 6 | 2 |
| α-helix | 629-633 | 5 | |
| α-helix | 640 | 1 | |
| β-strand | 641-645 | 5 | 2 |
| β-strand | 648-649 | 2 | 2 |
| α-helix | 655-665 | 11 | |
| β-strand | 676-683 | 8 | 2 |
Chain G: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 528-530 | 3 | 1 |
Chains H, I and L: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 530-531 | 2 | 2 |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Partitioning defective 3 homolog | A, B, C, D, E, F | protein | 112 | Rattus norvegicus | Q9Z340 (AlphaFold model) |
| INSC spindle orientation adaptor protein | G, H, I, J, K, L | protein | 10 | Mus musculus | D3Z267 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>9IMP_1 Partitioning defective 3 homolog (chains A, B, C, D, E, F)
GPGSEFPDGTREFLTFEVPLNDSGSAGLGVSVKGNRSKENHADLGIFVKSIINGGAASKD
GRLRVNDQLIAVNGESLLGKANQEAMETLRRSMSTEGNKRGMIQLIVARRIS
Sequence of entity 2 (G, H, I, J, K, L), FASTA
>9IMP_2 INSC spindle orientation adaptor protein (chains G, H, I, J, K, L)
LCSNMEESFV
Primary citation
mInsc coordinates Par3 and NuMA condensates for assembly of the spindle orientation machinery in asymmetric cell division. Huang, S., Fu, M., Gu, A. et al. Int J Biol Macromol (2024) 279:135126-135126. DOI 10.1016/j.ijbiomac.2024.135126 · PubMed
Other PDB entries of the same protein (UniProt Q9Z340 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6JUE 1.55 Å, The complex of PDZ and PBM
- 4DC2 2.4 Å, Structure of PKC in Complex with a Substrate Peptide from Par-3
- 4I6P 2.9 Å, Crystal structure of Par3-NTD domain
- 3ZEE 6.1 Å, Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain
- 2K1Z Solution structure of Par-3 PDZ3
- 2K20 Solution structure of Par-3 PDZ3 in complex with PTEN peptide
- 2NS5 The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for…
- 2OGP Solution structure of the second PDZ domain of Par-3
Browse structure collections
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