Crystal Structure Of Human G[alpha]i1 Bound To The Goloco Motif Of Rgs14. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Jul 2007.
Explore 2OM2 in 3D Show helices and sheets RCSB PDB PDBe
2OM2 contains 46 α-helices and 14 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 | 33-40 | 8 | 1 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-67 | 5 | |
| α-helix | 70-90 | 21 | |
| α-helix | 100-113 | 14 | |
| α-helix | 115 | 1 | |
| α-helix | 121-132 | 12 | |
| α-helix | 134-140 | 7 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-157 | 6 | |
| α-helix | 159-163 | 5 | |
| α-helix | 171-176 | 6 | |
| β-strand | 185-190 | 6 | 1 |
| β-strand | 195-200 | 6 | 1 |
| α-helix | 208-215 | 8 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 227-231 | 5 | |
| α-helix | 232-235 | 4 | |
| α-helix | 242-255 | 14 | |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 1 |
| α-helix | 271-277 | 7 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-308 | 13 | |
| β-strand | 319-323 | 5 | 1 |
| α-helix | 329-346 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 498-508 | 11 | |
| α-helix | 525-527 | 3 | |
| α-helix | 528-530 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1033-1039 | 7 | 2 |
| α-helix | 1048-1057 | 10 | |
| α-helix | 1063-1068 | 6 | |
| α-helix | 1070-1090 | 21 | |
| α-helix | 1100-1113 | 14 | |
| β-strand | 1115 | 1 | 3 |
| β-strand | 1118 | 1 | 3 |
| α-helix | 1121-1132 | 12 | |
| α-helix | 1134-1140 | 7 | |
| α-helix | 1143-1145 | 3 | |
| α-helix | 1152-1156 | 5 | |
| α-helix | 1159-1162 | 4 | |
| α-helix | 1171-1175 | 5 | |
| β-strand | 1185-1191 | 7 | 2 |
| β-strand | 1194-1200 | 7 | 2 |
| α-helix | 1208-1215 | 8 | |
| β-strand | 1220-1225 | 6 | 2 |
| α-helix | 1228-1231 | 4 | |
| α-helix | 1232-1235 | 4 | |
| α-helix | 1242-1255 | 14 | |
| α-helix | 1257-1259 | 3 | |
| β-strand | 1263-1268 | 6 | 2 |
| α-helix | 1271-1277 | 7 | |
| α-helix | 1283-1285 | 3 | |
| α-helix | 1296-1308 | 13 | |
| β-strand | 1319-1323 | 5 | 2 |
| α-helix | 1329-1345 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1497-1509 | 13 | |
| α-helix | 1521-1524 | 4 | |
| α-helix | 1525-1527 | 3 | |
| α-helix | 1528-1530 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(i), alpha-1 subunit | A, C | protein | 325 | Homo sapiens | P63096 (AlphaFold model) |
| Regulator of G-protein signalling 14 GoLoco motif peptide | B, D | protein | 36 | O43566 (AlphaFold model) |
>2OM2_1 Guanine nucleotide-binding protein G(i), alpha-1 subunit (chains A, C) GAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMG RLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLN DSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERK KWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLN KKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDT KNVQFVFDAVTDVIIKNNLKDCGLF
>2OM2_2 Regulator of G-protein signalling 14 GoLoco motif peptide (chains B, D) DIEGLVELLNRVQSSGAHDQRGLLRKEDLVLPEFLQ
Structure-based Protocol for Identifying Mutations that Enhance Protein-Protein Binding Affinities. Sammond, D.W., Eletr, Z.M., Purbeck, C. et al. J Mol Biol (2007) 371:1392-1404. DOI 10.1016/j.jmb.2007.05.096 · PubMed
Other PDB entries of the same protein (UniProt P63096 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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