6LES: PDB entry 6LES

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.

Method
X-ray diffraction
Resolution
2.0 Å
Organisms
Escherichia coli (strain K12), Homo sapiens
Chains
4
Atoms
11,755
Mol. weight
175.61 kDa
Released
11 Dec 2019

Explore 6LES in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 23 helices, 24 β-strands

ElementResiduesLengthSheet
β-strand8-1141
α-helix18-3215
β-strand36-3941
α-helix44-518
β-strand60-6451
α-helix66-738
β-strand7712
α-helix78-803
α-helix84-874
β-strand9013
α-helix92-976
β-strand99-10024
β-strand103-10424
β-strand107-11261
β-strand115-11955
β-strand12916
α-helix130-1323
α-helix133-1419
β-strand146-14835
α-helix155-16410
β-strand168-17367
α-helix174-1752
β-strand176-18388
α-helix187-20115
α-helix211-2199
β-strand223-22869
α-helix230-2323
α-helix233-2375
β-strand243-24649
α-helix247-2493
β-strand250110
β-strand251111
β-strand254111
β-strand259-260212
β-strand261-267713
β-strand268114
α-helix274-2807
α-helix281-2855
α-helix288-29710
β-strand302-303213
β-strand305115
α-helix306-3127
α-helix316-32712
β-strand329-330212
α-helix331-3322
α-helix337-35216
α-helix358-36912
Chains B and Y: 23 helices, 24 β-strands
ElementResiduesLengthSheet
β-strand8-11413
α-helix18-3215
β-strand36-39413
α-helix44-518
β-strand60-64513
α-helix65-739
β-strand77114
α-helix78-803
α-helix84-874
β-strand90115
α-helix92-976
β-strand99-100216
β-strand103-104216
β-strand107-112613
β-strand115-11959
β-strand129110
α-helix130-1323
α-helix133-1419
β-strand146-14839
α-helix155-16410
β-strand168-17368
α-helix174-1752
β-strand176-18387
α-helix187-20115
α-helix211-2199
β-strand223-22865
α-helix230-2323
α-helix233-2375
β-strand243-24645
α-helix247-2493
β-strand25016
β-strand251117
β-strand254117
β-strand259-260218
β-strand261-26771
β-strand26812
α-helix274-2807
α-helix281-2855
α-helix288-29710
β-strand302-30321
β-strand30513
α-helix306-3127
α-helix316-32712
β-strand329-330218
α-helix331-3322
α-helix337-35317
α-helix358-37114
Chain X: 23 helices, 24 β-strands
ElementResiduesLengthSheet
β-strand8-11419
α-helix18-3215
β-strand36-39419
α-helix44-518
β-strand60-64519
α-helix66-738
β-strand77120
α-helix78-803
α-helix84-874
β-strand90121
α-helix92-976
β-strand99-100222
β-strand103-104222
β-strand107-112619
β-strand115-119523
β-strand129124
α-helix130-1323
α-helix133-1419
β-strand146-148323
α-helix155-16410
β-strand168-173625
α-helix174-1752
β-strand176-183826
α-helix187-20115
α-helix211-2199
β-strand223-228627
α-helix230-2323
α-helix233-2375
β-strand243-246427
α-helix247-2493
β-strand250128
β-strand251129
β-strand254129
β-strand259-260230
β-strand261-267731
β-strand268132
α-helix274-2807
α-helix281-2855
α-helix288-29710
β-strand302-303231
β-strand305133
α-helix306-3127
α-helix316-32712
β-strand329-330230
α-helix331-3322
α-helix337-35317
α-helix358-36912

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose/maltodextrin-binding periplasmic protein,Focal adhesion kinase 1A, B, X, Yprotein397Escherichia coli (strain K12), Homo sapiensP0AEX9 (AlphaFold model), Q05397 (AlphaFold model)
Sequence of entity 1 (A, B, X, Y), FASTA
>6LES_1 Maltose/maltodextrin-binding periplasmic protein,Focal adhesion kinase 1 (chains A, B, X, Y)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA
ALAAAQTNATHLMEERLIRQQQEMEEDQRWLEKEERF

Primary citation

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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