3D domain-swapped dimer of the maltose-binding protein fused to a fragment of the focal adhesion kinase. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Dec 2019.
Explore 6LES in 3D Show helices and sheets RCSB PDB PDBe
6LES contains 92 α-helices and 96 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 | 8-11 | 4 | 1 |
| α-helix | 18-32 | 15 | |
| β-strand | 36-39 | 4 | 1 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-64 | 5 | 1 |
| α-helix | 66-73 | 8 | |
| β-strand | 77 | 1 | 2 |
| α-helix | 78-80 | 3 | |
| α-helix | 84-87 | 4 | |
| β-strand | 90 | 1 | 3 |
| α-helix | 92-97 | 6 | |
| β-strand | 99-100 | 2 | 4 |
| β-strand | 103-104 | 2 | 4 |
| β-strand | 107-112 | 6 | 1 |
| β-strand | 115-119 | 5 | 5 |
| β-strand | 129 | 1 | 6 |
| α-helix | 130-132 | 3 | |
| α-helix | 133-141 | 9 | |
| β-strand | 146-148 | 3 | 5 |
| α-helix | 155-164 | 10 | |
| β-strand | 168-173 | 6 | 7 |
| α-helix | 174-175 | 2 | |
| β-strand | 176-183 | 8 | 8 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-219 | 9 | |
| β-strand | 223-228 | 6 | 9 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-237 | 5 | |
| β-strand | 243-246 | 4 | 9 |
| α-helix | 247-249 | 3 | |
| β-strand | 250 | 1 | 10 |
| β-strand | 251 | 1 | 11 |
| β-strand | 254 | 1 | 11 |
| β-strand | 259-260 | 2 | 12 |
| β-strand | 261-267 | 7 | 13 |
| β-strand | 268 | 1 | 14 |
| α-helix | 274-280 | 7 | |
| α-helix | 281-285 | 5 | |
| α-helix | 288-297 | 10 | |
| β-strand | 302-303 | 2 | 13 |
| β-strand | 305 | 1 | 15 |
| α-helix | 306-312 | 7 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329-330 | 2 | 12 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-352 | 16 | |
| α-helix | 358-369 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 13 |
| α-helix | 18-32 | 15 | |
| β-strand | 36-39 | 4 | 13 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-64 | 5 | 13 |
| α-helix | 65-73 | 9 | |
| β-strand | 77 | 1 | 14 |
| α-helix | 78-80 | 3 | |
| α-helix | 84-87 | 4 | |
| β-strand | 90 | 1 | 15 |
| α-helix | 92-97 | 6 | |
| β-strand | 99-100 | 2 | 16 |
| β-strand | 103-104 | 2 | 16 |
| β-strand | 107-112 | 6 | 13 |
| β-strand | 115-119 | 5 | 9 |
| β-strand | 129 | 1 | 10 |
| α-helix | 130-132 | 3 | |
| α-helix | 133-141 | 9 | |
| β-strand | 146-148 | 3 | 9 |
| α-helix | 155-164 | 10 | |
| β-strand | 168-173 | 6 | 8 |
| α-helix | 174-175 | 2 | |
| β-strand | 176-183 | 8 | 7 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-219 | 9 | |
| β-strand | 223-228 | 6 | 5 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-237 | 5 | |
| β-strand | 243-246 | 4 | 5 |
| α-helix | 247-249 | 3 | |
| β-strand | 250 | 1 | 6 |
| β-strand | 251 | 1 | 17 |
| β-strand | 254 | 1 | 17 |
| β-strand | 259-260 | 2 | 18 |
| β-strand | 261-267 | 7 | 1 |
| β-strand | 268 | 1 | 2 |
| α-helix | 274-280 | 7 | |
| α-helix | 281-285 | 5 | |
| α-helix | 288-297 | 10 | |
| β-strand | 302-303 | 2 | 1 |
| β-strand | 305 | 1 | 3 |
| α-helix | 306-312 | 7 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329-330 | 2 | 18 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-353 | 17 | |
| α-helix | 358-371 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 19 |
| α-helix | 18-32 | 15 | |
| β-strand | 36-39 | 4 | 19 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-64 | 5 | 19 |
| α-helix | 66-73 | 8 | |
| β-strand | 77 | 1 | 20 |
| α-helix | 78-80 | 3 | |
| α-helix | 84-87 | 4 | |
| β-strand | 90 | 1 | 21 |
| α-helix | 92-97 | 6 | |
| β-strand | 99-100 | 2 | 22 |
| β-strand | 103-104 | 2 | 22 |
| β-strand | 107-112 | 6 | 19 |
| β-strand | 115-119 | 5 | 23 |
| β-strand | 129 | 1 | 24 |
| α-helix | 130-132 | 3 | |
| α-helix | 133-141 | 9 | |
| β-strand | 146-148 | 3 | 23 |
| α-helix | 155-164 | 10 | |
| β-strand | 168-173 | 6 | 25 |
| α-helix | 174-175 | 2 | |
| β-strand | 176-183 | 8 | 26 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-219 | 9 | |
| β-strand | 223-228 | 6 | 27 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-237 | 5 | |
| β-strand | 243-246 | 4 | 27 |
| α-helix | 247-249 | 3 | |
| β-strand | 250 | 1 | 28 |
| β-strand | 251 | 1 | 29 |
| β-strand | 254 | 1 | 29 |
| β-strand | 259-260 | 2 | 30 |
| β-strand | 261-267 | 7 | 31 |
| β-strand | 268 | 1 | 32 |
| α-helix | 274-280 | 7 | |
| α-helix | 281-285 | 5 | |
| α-helix | 288-297 | 10 | |
| β-strand | 302-303 | 2 | 31 |
| β-strand | 305 | 1 | 33 |
| α-helix | 306-312 | 7 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329-330 | 2 | 30 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-353 | 17 | |
| α-helix | 358-369 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,Focal adhesion kinase 1 | A, B, X, Y | protein | 397 | Escherichia coli (strain K12), Homo sapiens | P0AEX9 (AlphaFold model), Q05397 (AlphaFold model) |
>6LES_1 Maltose/maltodextrin-binding periplasmic protein,Focal adhesion kinase 1 (chains A, B, X, Y) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA ALAAAQTNATHLMEERLIRQQQEMEEDQRWLEKEERF
Passenger sequences can promote interlaced dimers in a common variant of the maltose-binding protein. Momin, A.A., Hameed, U.F.S., Arold, S.T. Sci Rep (2019) 9:20396-20396. DOI 10.1038/s41598-019-56718-y · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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