Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity. Determined by X-ray diffraction at 3.05 Å resolution. Released 19 May 2010.
Explore 3L8J in 3D Show helices and sheets RCSB PDB PDBe
3L8J contains 13 α-helices and 0 β-strands across 1 chain. 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 | 27-33 | 7 | |
| α-helix | 38-54 | 17 | |
| α-helix | 58-68 | 11 | |
| α-helix | 70-83 | 14 | |
| α-helix | 89-91 | 3 | |
| α-helix | 98-115 | 18 | |
| α-helix | 117-119 | 3 | |
| α-helix | 124-150 | 27 | |
| α-helix | 160-184 | 25 | |
| α-helix | 188-209 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Programmed cell death protein 10 | A | protein | 202 | Homo sapiens | Q9BUL8 (AlphaFold model) |
>3L8J_1 Programmed cell death protein 10 (chains A) XXXTTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGLTQDIIMKILEKK SVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIPDEINDRVRFLQT IKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTLKTYFKDGKAINV FVSANRLIHQTNLILQTFKTVA
Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity. Li, X., Zhang, R., Zhang, H. et al. J Biol Chem (2010) 285:24099-24107. DOI 10.1074/jbc.M110.128470 · 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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