Salmonella enterica SadA 1185-1386 fused to GCN4 adaptors (SadAK14). Determined by X-ray diffraction at 2.0 Å resolution. Released 12 Dec 2012.
Explore 2YO3 in 3D Show helices and sheets RCSB PDB PDBe
2YO3 contains 27 α-helices and 66 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 1158-1215 | 58 | |
| α-helix | 1216-1220 | 5 | |
| α-helix | 1221-1225 | 5 | |
| β-strand | 1231-1234 | 4 | 1 |
| α-helix | 1238-1240 | 3 | |
| β-strand | 1241-1242 | 2 | 2 |
| β-strand | 1248-1250 | 3 | 3 |
| β-strand | 1255-1256 | 2 | 2 |
| β-strand | 1262-1264 | 3 | 3 |
| β-strand | 1269-1270 | 2 | 2 |
| β-strand | 1275-1277 | 3 | 3 |
| β-strand | 1285 | 1 | 4 |
| β-strand | 1286-1288 | 3 | 1 |
| β-strand | 1290 | 1 | 5 |
| α-helix | 1291-1293 | 3 | |
| β-strand | 1299 | 1 | 6 |
| β-strand | 1301 | 1 | 7 |
| α-helix | 1302-1309 | 8 | |
| β-strand | 1312 | 1 | 8 |
| β-strand | 1314 | 1 | 9 |
| β-strand | 1316-1317 | 2 | 10 |
| β-strand | 1323-1324 | 2 | 10 |
| β-strand | 1327-1329 | 3 | 11 |
| β-strand | 1338 | 1 | 12 |
| β-strand | 1339-1341 | 3 | 13 |
| β-strand | 1343 | 1 | 14 |
| α-helix | 1344-1346 | 3 | |
| β-strand | 1352 | 1 | 15 |
| α-helix | 1353 | 1 | |
| β-strand | 1354 | 1 | 16 |
| α-helix | 1355-1411 | 57 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1157-1219 | 63 | |
| α-helix | 1222-1225 | 4 | |
| β-strand | 1231-1233 | 3 | 17 |
| α-helix | 1238-1240 | 3 | |
| β-strand | 1241-1242 | 2 | 18 |
| β-strand | 1247-1250 | 4 | 1 |
| β-strand | 1255-1256 | 2 | 18 |
| β-strand | 1262-1264 | 3 | 1 |
| β-strand | 1269-1270 | 2 | 18 |
| β-strand | 1275-1277 | 3 | 1 |
| β-strand | 1285 | 1 | 5 |
| β-strand | 1286-1288 | 3 | 17 |
| β-strand | 1290 | 1 | 19 |
| α-helix | 1291-1293 | 3 | |
| β-strand | 1299 | 1 | 20 |
| α-helix | 1300 | 1 | |
| β-strand | 1301 | 1 | 6 |
| α-helix | 1302-1310 | 9 | |
| β-strand | 1312 | 1 | 21 |
| β-strand | 1314 | 1 | 8 |
| α-helix | 1315 | 1 | |
| β-strand | 1316-1317 | 2 | 22 |
| α-helix | 1318 | 1 | |
| β-strand | 1323-1324 | 2 | 22 |
| β-strand | 1327-1329 | 3 | 13 |
| β-strand | 1338 | 1 | 14 |
| β-strand | 1339-1341 | 3 | 23 |
| β-strand | 1343 | 1 | 24 |
| α-helix | 1344-1346 | 3 | |
| β-strand | 1352 | 1 | 25 |
| β-strand | 1354 | 1 | 15 |
| α-helix | 1355-1411 | 57 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1157-1225 | 69 | |
| β-strand | 1231-1233 | 3 | 3 |
| α-helix | 1238-1240 | 3 | |
| β-strand | 1241-1242 | 2 | 26 |
| β-strand | 1248-1250 | 3 | 17 |
| β-strand | 1255-1256 | 2 | 26 |
| β-strand | 1262-1264 | 3 | 17 |
| β-strand | 1269-1270 | 2 | 26 |
| β-strand | 1275-1277 | 3 | 17 |
| β-strand | 1285 | 1 | 19 |
| β-strand | 1286-1288 | 3 | 3 |
| β-strand | 1290 | 1 | 4 |
| α-helix | 1291-1293 | 3 | |
| β-strand | 1299 | 1 | 7 |
| β-strand | 1301 | 1 | 20 |
| α-helix | 1302-1309 | 8 | |
| β-strand | 1312 | 1 | 9 |
| β-strand | 1314 | 1 | 21 |
| α-helix | 1315 | 1 | |
| β-strand | 1316-1317 | 2 | 27 |
| β-strand | 1323-1324 | 2 | 27 |
| β-strand | 1327-1329 | 3 | 23 |
| β-strand | 1338 | 1 | 24 |
| β-strand | 1339-1341 | 3 | 11 |
| β-strand | 1343 | 1 | 12 |
| α-helix | 1344-1346 | 3 | |
| β-strand | 1352 | 1 | 16 |
| α-helix | 1353 | 1 | |
| β-strand | 1354 | 1 | 25 |
| α-helix | 1355-1411 | 57 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| General control protein GCN4, putative inner membrane protein, general control protein GCN4 | A, B, C | protein | 268 | SACCHAROMYCES CEREVISIAE, SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM | P03069 (AlphaFold model), Q8ZL64 (AlphaFold model) |
>2YO3_1 GENERAL CONTROL PROTEIN GCN4, PUTATIVE INNER MEMBRANE PROTEIN, GENERAL CONTROL PROTEIN GCN4 (chains A, B, C) MKQIEDKIEEILSKIYHIENEIARIKKLIKVTDAQVSRNTQSITNLNTQVSNLDTRVTNI ENGIGDIVTTGSTKYFKTNTDGADANAQGADSVAIGSGSIAAAENSVALGTNSVADEANT VSVGSSTQQRRITNVAAGVNNTDAVNVAQLKASEAGSVRYETNADGSVNYSVLNLGDGSG GTTRIGNVSAAVNDTDAVNYAQLKRSVEEANTYTDQKMGEMNSKIKGVENKMKQIEDKIE EILSKIYHIENEIARIKKLIKLHHHHHH
Complete Fiber Structures of Complex Trimeric Autotransporter Adhesins Conserved in Enterobacteria. Hartmann, M.D., Grin, I., Dunin-Horkawicz, S. et al. Proc Natl Acad Sci U S A (2012) 109:20907. DOI 10.1073/PNAS.1211872110 · PubMed
Other PDB entries of the same protein (UniProt P03069 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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