Polypeptide Chain Release Factor 2 (RF2) from Escherichia coli. Determined by X-ray diffraction at 1.81 Å resolution. Released 4 Apr 2002.
Explore 1GQE in 3D Show helices and sheets RCSB PDB PDBe
1GQE contains 15 α-helices and 13 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 | 6-24 | 19 | |
| α-helix | 27-42 | 16 | |
| α-helix | 44-48 | 5 | |
| α-helix | 50-90 | 41 | |
| α-helix | 93-113 | 21 | |
| α-helix | 114-118 | 5 | |
| β-strand | 128-134 | 7 | 1 |
| α-helix | 138-158 | 21 | |
| β-strand | 162-170 | 9 | 1 |
| β-strand | 176-184 | 9 | 1 |
| α-helix | 188-192 | 5 | |
| α-helix | 193-195 | 3 | |
| β-strand | 197-204 | 8 | 1 |
| β-strand | 213-224 | 12 | 1 |
| β-strand | 227 | 1 | 2 |
| β-strand | 230 | 1 | 2 |
| α-helix | 236-238 | 3 | |
| β-strand | 239-244 | 6 | 3 |
| β-strand | 260-265 | 6 | 3 |
| β-strand | 271-274 | 4 | 3 |
| α-helix | 280-306 | 27 | |
| α-helix | 314-316 | 3 | |
| β-strand | 322-327 | 6 | 1 |
| α-helix | 328-330 | 3 | |
| β-strand | 332-335 | 4 | 1 |
| β-strand | 341-342 | 2 | 1 |
| α-helix | 345-349 | 5 | |
| α-helix | 354-362 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Release factor 2 | A | protein | 365 | ESCHERICHIA COLI | P07012 (AlphaFold model) |
>1GQE_1 RELEASE FACTOR 2 (chains A) MFEINPVNNRIQDLTERSDVLRGYLDYDAKKERLEEVNAELEQPDVWNEPERAQALGKER SSLEAVVDTLDQMKQGLEDVSGLLELAVEADDEETFNEAVAELDALEEKLAQLEFRRMFS GEYDSADCYLDIQAGSGGTEAQDWASMLERMYLRWAESRGFKTEIIEESEGEVAGIKSVT IKISGDYAYGWLRTETGVHRLVRKSPFDSGGRRHTSFSSAFVYPEVDDDIDIEINPADLR IDVYRASGAGGQHVNRTESAVRITHIPTGIVTQCQNDRSQHKNKDQAMKQMKAKLYEVEM QKKNAEKQAMEDNKSDIGWGSQIRSYVLDDSRIKDLRTGVETRNTQAVLDGSLDQFIEAS LKAGL
Bacterial Polypeptide Release Factor Rf2 is Structurally Distinct from Eukaryotic Erf1. Vestergaard, B., Van, L., Andersen, G. et al. Mol Cell (2001) 8:1375. DOI 10.1016/S1097-2765(01)00415-4 · PubMed
Other PDB entries of the same protein (UniProt P07012 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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