Crystal structure of the resting state maltose transporter from E. coli. Determined by X-ray diffraction at 4.5 Å resolution. Released 3 Mar 2009.
Explore 3FH6 in 3D Show helices and sheets RCSB PDB PDBe
3FH6 contains 120 α-helices and 118 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-10 | 7 | 1 |
| β-strand | 13 | 1 | 2 |
| β-strand | 16 | 1 | 2 |
| β-strand | 22-24 | 3 | 1 |
| β-strand | 32-35 | 4 | 3 |
| α-helix | 42-50 | 9 | |
| β-strand | 57-62 | 6 | 1 |
| β-strand | 66 | 1 | 1 |
| α-helix | 92-101 | 10 | |
| α-helix | 107-120 | 14 | |
| α-helix | 125-127 | 3 | |
| α-helix | 136-150 | 15 | |
| β-strand | 158 | 1 | 4 |
| α-helix | 166-183 | 18 | |
| β-strand | 190 | 1 | 4 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-207 | 5 | 3 |
| β-strand | 212-216 | 5 | 3 |
| α-helix | 218-222 | 5 | |
| β-strand | 227 | 1 | 5 |
| α-helix | 228-233 | 6 | |
| β-strand | 241-243 | 3 | 6 |
| β-strand | 256-257 | 2 | 7 |
| β-strand | 265-266 | 2 | 7 |
| β-strand | 282-284 | 3 | 6 |
| β-strand | 291 | 1 | 8 |
| β-strand | 301-304 | 4 | 9 |
| β-strand | 314-315 | 2 | 10 |
| β-strand | 318-319 | 2 | 9 |
| β-strand | 330-331 | 2 | 10 |
| β-strand | 342-344 | 3 | 9 |
| β-strand | 346 | 1 | 8 |
| β-strand | 355 | 1 | 6 |
| β-strand | 360 | 1 | 5 |
| β-strand | 361 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-10 | 7 | 11 |
| β-strand | 13 | 1 | 12 |
| β-strand | 16 | 1 | 12 |
| β-strand | 20-24 | 5 | 11 |
| β-strand | 32-35 | 4 | 13 |
| α-helix | 42-50 | 9 | |
| β-strand | 57-62 | 6 | 11 |
| α-helix | 67-69 | 3 | |
| α-helix | 73-75 | 3 | |
| β-strand | 77-79 | 3 | 14 |
| α-helix | 92-96 | 5 | |
| α-helix | 99-103 | 5 | |
| α-helix | 107-120 | 14 | |
| α-helix | 125-127 | 3 | |
| α-helix | 136-150 | 15 | |
| β-strand | 154-156 | 3 | 14 |
| β-strand | 158 | 1 | 15 |
| α-helix | 160-162 | 3 | |
| α-helix | 166-183 | 18 | |
| β-strand | 190 | 1 | 15 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-206 | 4 | 13 |
| β-strand | 214-216 | 3 | 13 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 16 |
| α-helix | 228-233 | 6 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240 | 1 | 17 |
| β-strand | 249-250 | 2 | 18 |
| β-strand | 253-254 | 2 | 18 |
| β-strand | 256 | 1 | 19 |
| β-strand | 266 | 1 | 19 |
| β-strand | 270 | 1 | 20 |
| β-strand | 282-284 | 3 | 21 |
| β-strand | 285 | 1 | 17 |
| β-strand | 291 | 1 | 22 |
| β-strand | 301-306 | 6 | 23 |
| β-strand | 314 | 1 | 24 |
| β-strand | 317-319 | 3 | 23 |
| α-helix | 326 | 1 | |
| β-strand | 327 | 1 | 23 |
| β-strand | 331 | 1 | 24 |
| β-strand | 342-344 | 3 | 23 |
| β-strand | 346 | 1 | 22 |
| β-strand | 353-355 | 3 | 21 |
| β-strand | 360 | 1 | 16 |
| β-strand | 361 | 1 | 21 |
| β-strand | 364 | 1 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42-55 | 14 | |
| α-helix | 68-74 | 7 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-87 | 7 | |
| α-helix | 102-110 | 9 | |
| α-helix | 265-268 | 4 | |
| α-helix | 276-306 | 31 | |
| α-helix | 314-326 | 13 | |
| α-helix | 330-339 | 10 | |
| α-helix | 346-354 | 9 | |
| α-helix | 365-394 | 30 | |
| α-helix | 397-406 | 10 | |
| α-helix | 411-412 | 2 | |
| α-helix | 413-418 | 6 | |
| α-helix | 423-438 | 16 | |
| α-helix | 441-447 | 7 | |
| α-helix | 451 | 1 | |
| α-helix | 453 | 1 | |
| α-helix | 467-473 | 7 | |
| α-helix | 487-507 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-26 | 18 | |
| α-helix | 29-35 | 7 | |
| α-helix | 81-111 | 31 | |
| α-helix | 118-129 | 12 | |
| α-helix | 136-150 | 15 | |
| α-helix | 159-166 | 8 | |
| α-helix | 167-169 | 3 | |
| α-helix | 170-183 | 14 | |
| α-helix | 187-194 | 8 | |
| α-helix | 199-201 | 3 | |
| α-helix | 202-207 | 6 | |
| α-helix | 212-227 | 16 | |
| α-helix | 231-236 | 6 | |
| α-helix | 245-248 | 4 | |
| α-helix | 249-251 | 3 | |
| α-helix | 260-283 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose transport system permease protein malF | F, H | protein | 480 | Escherichia coli | P02916 (AlphaFold model) |
| Maltose transport system permease protein malG | G, I | protein | 296 | Escherichia coli | P68183 (AlphaFold model) |
| Maltose/maltodextrin import ATP-binding protein malK | A, B, C, D | protein | 381 | Escherichia coli | P68187 (AlphaFold model) |
>3FH6_1 Maltose transport system permease protein malF (chains F, H) MAQGEYLFAITTLILSSAGLYIFANRKAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNY SSTNQLTFERAQEVLLDRSWQAGKTYNFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGE QKLQLKETTAQPEGERANLRVITQNRQALSDITAILPDGNKVMMSSLRQFSGTQPLYTLD GDGTLTNNQSGVKYRPNNQIGFYQSITADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQ KPFLAIFVWTVVFSLITVFLTVAVGMVLACLVQWEALRGKAVYRVLLILPYAVPSFISIL IFKGLFNQSFGEINMMLSALFGVKPAWFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKA IPDDLYEASAMDGAGPFQNFFKITLPLLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDR LGTTTPAGYTDLLVNYTYRIAFEGGGGQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD
>3FH6_2 Maltose transport system permease protein malG (chains G, I) MAMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLIPEQISWDHWK LALGFSVEQADGRITPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKAT LLKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGY FETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDV NSYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVNGLTAGGVKG
>3FH6_3 Maltose/maltodextrin import ATP-binding protein malK (chains A, B, C, D) MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL FIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEV LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN FLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVIL EGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGT ACRRLHKEPGVASASHHHHHH
Alternating access in maltose transporter mediated by rigid-body rotations. Khare, D., Oldham, M.L., Orelle, C. et al. Mol Cell (2009) 33:528-536. DOI 10.1016/j.molcel.2009.01.035 · PubMed
Other PDB entries of the same protein (UniProt P02916 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3FH6 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.