Crystal structure of the G202D mutant of human G-alpha-i1. Determined by X-ray diffraction at 2.04 Å resolution. Released 24 Oct 2012.
Explore 3UMR in 3D Show helices and sheets RCSB PDB PDBe
3UMR contains 22 α-helices and 7 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 | 9-16 | 8 | |
| α-helix | 20-23 | 4 | |
| α-helix | 27-29 | 3 | |
| α-helix | 30-31 | 2 | |
| β-strand | 32-40 | 9 | 1 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-67 | 5 | |
| α-helix | 70-91 | 22 | |
| α-helix | 100-113 | 14 | |
| α-helix | 121-132 | 12 | |
| α-helix | 134-140 | 7 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-157 | 6 | |
| α-helix | 159-162 | 4 | |
| α-helix | 171-175 | 5 | |
| β-strand | 184-191 | 8 | 1 |
| β-strand | 194-201 | 8 | 1 |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 227-229 | 3 | |
| α-helix | 242-254 | 13 | |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 1 |
| α-helix | 271-277 | 7 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-309 | 14 | |
| β-strand | 319-323 | 5 | 1 |
| α-helix | 329-346 | 18 | |
| α-helix | 348-350 | 3 | |
| β-strand | 353 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(i) subunit alpha-1 | A | protein | 354 | Homo sapiens | P63096 (AlphaFold model) |
>3UMR_1 Guanine nucleotide-binding protein G(i) subunit alpha-1 (chains A) MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAG YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK TTGIVETHFTFKDLHFKMFDVDGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM NRMHESMKLFDSICNNKCFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAA AYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
Water and common crystallization additives (SO4, CL, GOL) are not listed.
Structural Determinants Underlying the Temperature-sensitive Nature of a G-alpha Mutant in Asymmetric Cell Division of Caenorhabditis elegans. Johnston, C.A., Afshar, K., Snyder, J.T. et al. To be published.
Other PDB entries of the same protein (UniProt P63096 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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