Crystal structure of programmed cell death 10 in complex with inositol 1,3,4,5-tetrakisphosphate. Determined by X-ray diffraction at 2.3 Å resolution. Released 30 Jun 2010.
Explore 3AJM in 3D Show helices and sheets RCSB PDB PDBe
3AJM contains 25 α-helices and 0 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 | 17-19 | 3 | |
| α-helix | 20-21 | 2 | |
| α-helix | 22-26 | 5 | |
| α-helix | 27-36 | 10 | |
| α-helix | 38-54 | 17 | |
| α-helix | 58-68 | 11 | |
| α-helix | 70-83 | 14 | |
| α-helix | 84-86 | 3 | |
| α-helix | 98-115 | 18 | |
| α-helix | 117-120 | 4 | |
| α-helix | 124-151 | 28 | |
| α-helix | 157-184 | 28 | |
| α-helix | 187-210 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-19 | 3 | |
| α-helix | 20-21 | 2 | |
| α-helix | 22-26 | 5 | |
| α-helix | 27-33 | 7 | |
| α-helix | 38-54 | 17 | |
| α-helix | 58-68 | 11 | |
| α-helix | 70-83 | 14 | |
| α-helix | 98-115 | 18 | |
| α-helix | 117-119 | 3 | |
| α-helix | 124-149 | 26 | |
| α-helix | 158-184 | 27 | |
| α-helix | 187-207 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Programmed cell death protein 10 | A, B | protein | 213 | Homo sapiens | Q9BUL8 (AlphaFold model) |
>3AJM_1 Programmed cell death protein 10 (chains A, B) MKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGLTQDIIMKIL EKKSVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIPDEINDRVRF LQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTLKTYFKDGKA INVFVSANRLIHQTNLILQTFKTVALEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| 4IP | Inositol-(1,3,4,5)-tetrakisphosphate | C6 H16 O18 P4 | 1 |
Crystal structure of human programmed cell death 10 complexed with inositol-(1,3,4,5)-tetrakisphosphate: a novel adaptor protein involved in human cerebral cavernous malformation. Ding, J., Wang, X., Li, D.F. et al. Biochem Biophys Res Commun (2010) 399:587-592. DOI 10.1016/j.bbrc.2010.07.119 · PubMed
Other PDB entries of the same protein (UniProt Q9BUL8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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