Crystal structure of the DHR-2 domain of DOCK8 in complex with Cdc42 (T17N mutant). Determined by X-ray diffraction at 2.08 Å resolution. Released 20 Jun 2012.
Explore 3VHL in 3D Show helices and sheets RCSB PDB PDBe
3VHL contains 27 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 |
|---|---|---|---|
| β-strand | 1794-1801 | 8 | 1 |
| α-helix | 1803-1808 | 6 | |
| β-strand | 1812-1817 | 6 | 1 |
| α-helix | 1823-1838 | 16 | |
| α-helix | 1840-1842 | 3 | |
| β-strand | 1843-1846 | 4 | 1 |
| α-helix | 1851-1852 | 2 | |
| α-helix | 1854-1856 | 3 | |
| β-strand | 1862-1869 | 8 | 1 |
| β-strand | 1870-1871 | 2 | 2 |
| α-helix | 1875-1878 | 4 | |
| β-strand | 1891-1900 | 10 | 2 |
| α-helix | 1910-1912 | 3 | |
| β-strand | 1914-1926 | 13 | 2 |
| β-strand | 1932-1934 | 3 | 1 |
| β-strand | 1935-1943 | 9 | 2 |
| α-helix | 1945-1965 | 21 | |
| α-helix | 1971-1982 | 12 | |
| α-helix | 1990-1997 | 8 | |
| α-helix | 2005-2035 | 31 | |
| α-helix | 2038-2040 | 3 | |
| α-helix | 2041-2062 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3 | 1 | |
| β-strand | 4-10 | 7 | 3 |
| α-helix | 16-25 | 10 | |
| α-helix | 29-31 | 3 | |
| α-helix | 32-34 | 3 | |
| β-strand | 40-46 | 7 | 3 |
| β-strand | 49-57 | 9 | 3 |
| α-helix | 62-64 | 3 | |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 3 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 3 |
| α-helix | 117-120 | 4 | |
| α-helix | 123-131 | 9 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-149 | 11 | |
| β-strand | 153-156 | 4 | 3 |
| α-helix | 165-176 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dedicator of cytokinesis protein 8 | A | protein | 288 | Mus musculus | Q8C147 (AlphaFold model) |
| Cell division control protein 42 homolog | B | protein | 195 | Homo sapiens | P60953 (AlphaFold model) |
>3VHL_1 Dedicator of cytokinesis protein 8 (chains A) GSSGSSGDHKRMFGTYFRVGFYGSRFGDLDEQEFVYKEPAITKLPEISHRLEGFYGQCFG AEFVEVIKDSTPVDKTKLDPNKAYIQITFVEPYFDEYEMKDRVTYFEKNFNLRRFMYTTP FTLEGRPRGELHEQHRRNTVLTTMHAFPYIKTRIRVSQKEEFVLTPIEVAIEDMKKKTLQ LAVATHQEPPDAKMLQMVLQGSVGATVNQGPLEVAQVFLAEIPADPKLYRHHNKLRLCFK EFIMRCGEAVEKNRRLITAEQREYQQELKKNYNKLRDSLRPMIERKIP
>3VHL_2 Cell division control protein 42 homolog (chains B) GSSGSSGMQTIKCVVVGDGAVGKNCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTL GLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLV GTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAI LAALEPPEPKKSRRS
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 2 |
DOCK8 is a Cdc42 activator critical for interstitial dendritic cell migration during immune responses. Harada, Y., Tanaka, Y., Terasawa, M. et al. Blood (2012) 119:4451-4461. DOI 10.1182/blood-2012-01-407098 · PubMed
Other PDB entries of the same protein (UniProt Q8C147 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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