Gtpase-activation domain from rhogap. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Oct 1997.
Explore 1RGP in 3D Show helices and sheets RCSB PDB PDBe
1RGP contains 15 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 | 49-55 | 7 | |
| α-helix | 64-76 | 13 | |
| α-helix | 90-101 | 12 | |
| α-helix | 104-106 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 115-126 | 12 | |
| α-helix | 135-137 | 3 | |
| α-helix | 138-142 | 5 | |
| α-helix | 149-151 | 3 | |
| α-helix | 152-160 | 9 | |
| α-helix | 165-182 | 18 | |
| α-helix | 185-188 | 4 | |
| α-helix | 192-203 | 12 | |
| α-helix | 217-228 | 12 | |
| α-helix | 230-233 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rhogap | A | protein | 242 | Homo sapiens | Q07960 (AlphaFold model) |
>1RGP_1 RHOGAP (chains A) HVKLEQLGIPRQVLKYDDFLKSTQKSPATAPKPMPPRPPLPNQQFGVSLQHLQEKNPEQE PIPIVLRETVAYLQAHALTTEGIFRRSANTQVVREVQQKYNMGLPVDFDQYNELHLPAVI LKTFLRELPEPLLTFDLYPHVVGFLNIDESQRVPATLQVLQTLPEENYQVLRFLTAFLVQ ISAHSDQNKMTNTNLAVVFGPNLLWAKDAAITLKAINPINTFTKFLLDHQGELFPSPDPS GL
The structure of the GTPase-activating domain from p50rhoGAP. Barrett, T., Xiao, B., Dodson, E.J. et al. Nature (1997) 385:458-461. DOI 10.1038/385458a0 · PubMed
Other PDB entries of the same protein (UniProt Q07960 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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