Rac1-RhoGDI complex involved in NADPH oxidase activation. Determined by X-ray diffraction at 2.7 Å resolution. Released 28 Aug 2001.
Explore 1HH4 in 3D Show helices and sheets RCSB PDB PDBe
1HH4 contains 35 α-helices and 37 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 |
|---|---|---|---|
| β-strand | 2 | 1 | 1 |
| β-strand | 5-10 | 6 | 1 |
| α-helix | 16-24 | 9 | |
| α-helix | 37-39 | 3 | |
| β-strand | 40-45 | 6 | 1 |
| β-strand | 50-57 | 8 | 1 |
| α-helix | 62-64 | 3 | |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 1 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 1 |
| α-helix | 117-119 | 3 | |
| α-helix | 125-128 | 4 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-149 | 11 | |
| β-strand | 153-156 | 4 | 1 |
| β-strand | 158 | 1 | 2 |
| β-strand | 163 | 1 | 2 |
| α-helix | 165-176 | 12 | |
| α-helix | 180-182 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-10 | 9 | 3 |
| α-helix | 16-24 | 9 | |
| β-strand | 42-45 | 4 | 3 |
| β-strand | 50-57 | 8 | 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 | 117-119 | 3 | |
| α-helix | 125-128 | 4 | |
| α-helix | 130-132 | 3 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-149 | 11 | |
| β-strand | 153-156 | 4 | 3 |
| β-strand | 158 | 1 | 4 |
| β-strand | 163 | 1 | 4 |
| α-helix | 165-176 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 328-331 | 4 | |
| α-helix | 335-339 | 5 | |
| α-helix | 346-356 | 11 | |
| β-strand | 370-379 | 10 | 5 |
| β-strand | 387-389 | 3 | 5 |
| α-helix | 395-398 | 4 | |
| β-strand | 401-404 | 4 | 6 |
| β-strand | 409-418 | 10 | 5 |
| β-strand | 423-433 | 11 | 6 |
| β-strand | 438-449 | 12 | 6 |
| β-strand | 456-459 | 4 | 5 |
| α-helix | 460-462 | 3 | |
| β-strand | 463-464 | 2 | 5 |
| β-strand | 474-482 | 9 | 6 |
| β-strand | 490-498 | 9 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 329-331 | 3 | |
| α-helix | 335-339 | 5 | |
| α-helix | 346-356 | 11 | |
| β-strand | 370-379 | 10 | 7 |
| β-strand | 386-389 | 4 | 7 |
| α-helix | 395-398 | 4 | |
| β-strand | 401-405 | 5 | 8 |
| β-strand | 409-418 | 10 | 7 |
| β-strand | 423-433 | 11 | 8 |
| β-strand | 438-449 | 12 | 8 |
| β-strand | 456-459 | 4 | 7 |
| α-helix | 460-462 | 3 | |
| β-strand | 463-464 | 2 | 7 |
| α-helix | 468-471 | 4 | |
| β-strand | 474-482 | 9 | 8 |
| β-strand | 490-499 | 10 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ras-related C3 botulinum toxin substrate 1 | A, B | protein | 192 | HOMO SAPIENS | P63000 (AlphaFold model) |
| Rho GDP-dissociation inhibitor 1 | D, E | protein | 204 | HOMO SAPIENS | P52565 (AlphaFold model) |
>1HH4_1 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 (chains A, B) PQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG QEDYDRLRPLSYPQTDVSLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP PVKKRKRKCLLL
>1HH4_2 RHO GDP-DISSOCIATION INHIBITOR 1 (chains D, E) MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVA VSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNR EIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSR FTDDDKTDHLSWEWNLTIKKDWKD
| ID | Name | Formula | Copies |
|---|---|---|---|
| GER | Geran-8-yl geran | C20 H34 | 2 |
| MG | Magnesium ion | Mg | 2 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
Crystal Structure of the Rac1-Rhogdi Complex Involved in Nadph Oxidase Activation. Grizot, S., Faure, J., Fieschi, F. et al. Biochemistry (2001) 40:10007. DOI 10.1021/BI010288K · PubMed
Other PDB entries of the same protein (UniProt P63000 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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