A Complex between PH Domain of LbcRhoGEF (AKAP-Lbc) and Activated RhoA Bound to a GTP Analog. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Dec 2017.
Explore 6BCA in 3D Show helices and sheets RCSB PDB PDBe
6BCA contains 33 α-helices and 38 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 | 2194-2207 | 14 | |
| β-strand | 2208 | 1 | 2 |
| β-strand | 2213-2215 | 3 | 3 |
| α-helix | 2220 | 1 | |
| β-strand | 2221-2223 | 3 | 3 |
| α-helix | 2224-2227 | 4 | |
| β-strand | 2232-2241 | 10 | 2 |
| β-strand | 2247-2255 | 9 | 2 |
| β-strand | 2258-2265 | 8 | 2 |
| β-strand | 2268-2271 | 4 | 2 |
| α-helix | 2272-2273 | 2 | |
| β-strand | 2274 | 1 | 4 |
| β-strand | 2277 | 1 | 4 |
| β-strand | 2280-2282 | 3 | 2 |
| β-strand | 2286-2290 | 5 | 2 |
| β-strand | 2297-2302 | 6 | 2 |
| β-strand | 2309-2314 | 6 | 2 |
| α-helix | 2318-2332 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2197-2207 | 11 | |
| β-strand | 2208 | 1 | 5 |
| β-strand | 2213-2215 | 3 | 6 |
| α-helix | 2220 | 1 | |
| β-strand | 2221-2223 | 3 | 6 |
| α-helix | 2224-2227 | 4 | |
| β-strand | 2232-2241 | 10 | 5 |
| α-helix | 2242 | 1 | |
| β-strand | 2247-2255 | 9 | 5 |
| β-strand | 2258-2265 | 8 | 5 |
| β-strand | 2268-2271 | 4 | 5 |
| α-helix | 2272-2273 | 2 | |
| β-strand | 2274 | 1 | 7 |
| β-strand | 2277 | 1 | 7 |
| β-strand | 2280-2282 | 3 | 5 |
| β-strand | 2286-2290 | 5 | 5 |
| β-strand | 2297-2302 | 6 | 5 |
| β-strand | 2309-2314 | 6 | 5 |
| α-helix | 2318-2332 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-12 | 9 | 8 |
| α-helix | 18-27 | 10 | |
| β-strand | 39-48 | 10 | 8 |
| β-strand | 51-60 | 10 | 8 |
| α-helix | 64-66 | 3 | |
| α-helix | 70-73 | 4 | |
| β-strand | 79-85 | 7 | 8 |
| α-helix | 89-94 | 6 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-106 | 7 | |
| β-strand | 112-117 | 6 | 8 |
| α-helix | 119-121 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-151 | 11 | |
| β-strand | 155-158 | 4 | 8 |
| α-helix | 167-179 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-12 | 9 | 1 |
| α-helix | 18-27 | 10 | |
| β-strand | 39-48 | 10 | 1 |
| β-strand | 51-60 | 10 | 1 |
| α-helix | 64-66 | 3 | |
| α-helix | 70-73 | 4 | |
| β-strand | 79-85 | 7 | 1 |
| α-helix | 89-94 | 6 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-106 | 7 | |
| β-strand | 112-117 | 6 | 1 |
| α-helix | 119-121 | 3 | |
| α-helix | 125-132 | 8 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-151 | 11 | |
| β-strand | 155-158 | 4 | 1 |
| α-helix | 167-179 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming protein RhoA | C, F | protein | 185 | Homo sapiens | P61586 (AlphaFold model) |
| A-kinase anchor protein 13 | A, B | protein | 151 | Homo sapiens | Q12802 (AlphaFold model) |
>6BCA_1 Transforming protein RhoA (chains C, F) GILDMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELA LWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVG NKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATR AALQA
>6BCA_2 A-kinase anchor protein 13 (chains A, B) GILDASYEKKVRLNEIYTKTDSKSIMRMKSGQMFAKEDLKRKKLVRDGSVFLKNAAGRLK EVQAVLLTDILVFLQEKDQKYIFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMTDP EMVEVHASSKEERNSWIQIIQDTINHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| GSP | 5'-guanosine-diphosphate-monothiophosphate | C10 H16 N5 O13 P3 S | 2 |
Crystal structures of the PH domains from Lbc family of RhoGEFs bound to activated RhoA GTPase. Chen, Z., Gutowski, S., Sternweis, P.C. Data Brief (2018) 17:356-362. DOI 10.1016/j.dib.2018.01.024 · PubMed
Other PDB entries of the same protein (UniProt P61586 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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