1FOE: RAC1
Crystal structure of RAC1 in complex with the guanine nucleotide exchange region of TIAM1. Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Jan 2001.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organisms
- Mus musculus, Homo sapiens
- Chains
- 8
- Atoms
- 17,570
- Mol. weight
- 254.54 kDa
- Released
- 17 Jan 2001
Explore 1FOE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1FOE contains 129 α-helices and 60 β-strands across 8 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.
Chain A: 22 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1037-1062 | 26 | |
| α-helix | 1063-1067 | 5 | |
| α-helix | 1068-1071 | 4 | |
| α-helix | 1078-1085 | 8 | |
| α-helix | 1088-1106 | 19 | |
| α-helix | 1112-1114 | 3 | |
| α-helix | 1118-1121 | 4 | |
| α-helix | 1122-1135 | 14 | |
| α-helix | 1138-1141 | 4 | |
| α-helix | 1142-1148 | 7 | |
| α-helix | 1152-1156 | 5 | |
| α-helix | 1163-1172 | 10 | |
| α-helix | 1178-1180 | 3 | |
| α-helix | 1182-1185 | 4 | |
| α-helix | 1188-1193 | 6 | |
| α-helix | 1196-1205 | 10 | |
| α-helix | 1212-1249 | 38 | |
| α-helix | 1264-1266 | 3 | |
| β-strand | 1267-1275 | 9 | 1 |
| α-helix | 1280-1283 | 4 | |
| β-strand | 1290-1296 | 7 | 1 |
| β-strand | 1299-1304 | 6 | 1 |
| β-strand | 1332-1336 | 5 | 1 |
| α-helix | 1337-1339 | 3 | |
| β-strand | 1340-1343 | 4 | 1 |
| β-strand | 1355-1360 | 6 | 1 |
| β-strand | 1363 | 1 | 2 |
| α-helix | 1365-1367 | 3 | |
| β-strand | 1368 | 1 | 2 |
| β-strand | 1371-1377 | 7 | 1 |
| α-helix | 1380-1400 | 21 | |
Chains B, F and H: 11 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-9 | 7 | 3 |
| α-helix | 16-25 | 10 | |
| α-helix | 38-39 | 2 | |
| β-strand | 40-46 | 7 | 3 |
| β-strand | 49-56 | 8 | 3 |
| α-helix | 68-70 | 3 | |
| 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 | 123-131 | 9 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 153-156 | 4 | 3 |
| α-helix | 165-176 | 12 | |
Chain C: 21 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1037-1062 | 26 | |
| α-helix | 1063-1067 | 5 | |
| α-helix | 1068-1071 | 4 | |
| α-helix | 1078-1085 | 8 | |
| α-helix | 1088-1106 | 19 | |
| α-helix | 1112-1114 | 3 | |
| α-helix | 1118-1121 | 4 | |
| α-helix | 1122-1135 | 14 | |
| α-helix | 1138-1141 | 4 | |
| α-helix | 1142-1148 | 7 | |
| α-helix | 1152-1156 | 5 | |
| α-helix | 1163-1172 | 10 | |
| α-helix | 1178-1180 | 3 | |
| α-helix | 1182-1185 | 4 | |
| α-helix | 1188-1193 | 6 | |
| α-helix | 1196-1205 | 10 | |
| α-helix | 1212-1249 | 38 | |
| β-strand | 1267-1275 | 9 | 4 |
| α-helix | 1280-1283 | 4 | |
| β-strand | 1290-1296 | 7 | 4 |
| β-strand | 1299-1305 | 7 | 4 |
| β-strand | 1329-1336 | 8 | 4 |
| α-helix | 1337-1339 | 3 | |
| β-strand | 1340-1343 | 4 | 4 |
| β-strand | 1355-1360 | 6 | 4 |
| β-strand | 1363 | 1 | 5 |
| α-helix | 1365-1367 | 3 | |
| β-strand | 1368 | 1 | 5 |
| β-strand | 1371-1377 | 7 | 4 |
| α-helix | 1380-1396 | 17 | |
Chain D: 11 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-9 | 7 | 6 |
| α-helix | 16-25 | 10 | |
| α-helix | 38-39 | 2 | |
| β-strand | 40-46 | 7 | 6 |
| β-strand | 49-56 | 8 | 6 |
| α-helix | 68-70 | 3 | |
| β-strand | 77-83 | 7 | 6 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 6 |
| α-helix | 117-119 | 3 | |
| α-helix | 123-130 | 8 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 153-156 | 4 | 6 |
| α-helix | 165-176 | 12 | |
Chain E: 21 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1037-1062 | 26 | |
| α-helix | 1063-1067 | 5 | |
| α-helix | 1068-1071 | 4 | |
| α-helix | 1078-1085 | 8 | |
| α-helix | 1088-1106 | 19 | |
| α-helix | 1112-1114 | 3 | |
| α-helix | 1118-1121 | 4 | |
| α-helix | 1122-1135 | 14 | |
| α-helix | 1138-1141 | 4 | |
| α-helix | 1142-1148 | 7 | |
| α-helix | 1152-1156 | 5 | |
| α-helix | 1163-1172 | 10 | |
| α-helix | 1178-1180 | 3 | |
| α-helix | 1182-1185 | 4 | |
| α-helix | 1188-1205 | 18 | |
| α-helix | 1212-1249 | 38 | |
| α-helix | 1264-1266 | 3 | |
| β-strand | 1267-1275 | 9 | 7 |
| α-helix | 1280-1283 | 4 | |
| β-strand | 1290-1296 | 7 | 7 |
| β-strand | 1299-1304 | 6 | 7 |
| β-strand | 1332-1336 | 5 | 7 |
| α-helix | 1337-1339 | 3 | |
| β-strand | 1340-1343 | 4 | 7 |
| β-strand | 1355-1360 | 6 | 7 |
| β-strand | 1363 | 1 | 8 |
| α-helix | 1365-1367 | 3 | |
| β-strand | 1368 | 1 | 8 |
| β-strand | 1371-1377 | 7 | 7 |
| α-helix | 1380-1400 | 21 | |
Chain G: 21 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1037-1062 | 26 | |
| α-helix | 1063-1067 | 5 | |
| α-helix | 1068-1071 | 4 | |
| α-helix | 1078-1085 | 8 | |
| α-helix | 1088-1106 | 19 | |
| α-helix | 1112-1114 | 3 | |
| α-helix | 1118-1121 | 4 | |
| α-helix | 1122-1135 | 14 | |
| α-helix | 1138-1141 | 4 | |
| α-helix | 1142-1148 | 7 | |
| α-helix | 1152-1156 | 5 | |
| α-helix | 1163-1172 | 10 | |
| α-helix | 1178-1180 | 3 | |
| α-helix | 1182-1185 | 4 | |
| α-helix | 1188-1193 | 6 | |
| α-helix | 1196-1205 | 10 | |
| α-helix | 1212-1249 | 38 | |
| β-strand | 1267-1275 | 9 | 10 |
| α-helix | 1280-1283 | 4 | |
| β-strand | 1290-1296 | 7 | 10 |
| β-strand | 1299-1304 | 6 | 10 |
| β-strand | 1331-1336 | 6 | 10 |
| α-helix | 1337-1339 | 3 | |
| β-strand | 1340-1343 | 4 | 10 |
| β-strand | 1355-1360 | 6 | 10 |
| β-strand | 1363 | 1 | 11 |
| α-helix | 1365-1367 | 3 | |
| β-strand | 1368 | 1 | 11 |
| β-strand | 1371-1376 | 6 | 10 |
| α-helix | 1380-1398 | 19 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| T-lymphoma invasion and metastasis inducing protein 1 | A, C, E, G | protein | 377 | Mus musculus | Q60610 (AlphaFold model) |
| Ras-related C3 botulinum toxin substrate | B, D, F, H | protein | 177 | Homo sapiens | P63000 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>1FOE_1 T-LYMPHOMA INVASION AND METASTASIS INDUCING PROTEIN 1 (chains A, C, E, G)
AMGRQLSDADKLRKVICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLT
EMVEFQVEFLKTLEDGVRLVPDLEKLEKVDQFKKVLFSLGGSFLYYADRFKLYSAFCASH
TKVPKVLVKAKTDTAFKAFLDAQNPRQQHSSTLESYLIKPIQRVLKYPLLLRELFALTDA
ESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLL
HTSVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKLVGSHRLSIYEEWDPF
RFRHMIPTEALQVRALPSADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKS
VHSILRDKHRRQLLKTE
Sequence of entity 2 (B, D, F, H), FASTA
>1FOE_2 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE (chains B, D, F, H)
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVL
Primary citation
Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Worthylake, D.K., Rossman, K.L., Sondek, J. Nature (2000) 408:682-688. DOI 10.1038/35047014 · PubMed
Other PDB entries of the same protein (UniProt Q60610 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7UIR 3.1 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and Tiam1 in complex…
- 7UIQ 3.11 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and Tiam1
- 3A8N 4.5 Å, Crystal structure of the Tiam1 PHCCEx domain
Browse structure collections
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