Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2. Determined by electron microscopy at 3.34 Å resolution. Released 24 Sept 2025.
Explore 9NQJ in 3D Show helices and sheets RCSB PDB PDBe
9NQJ contains 60 α-helices and 55 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 | 4-13 | 10 | 1 |
| β-strand | 16-26 | 11 | 1 |
| β-strand | 32-35 | 4 | 2 |
| α-helix | 42-50 | 9 | |
| β-strand | 59-62 | 4 | 1 |
| β-strand | 66 | 1 | 1 |
| β-strand | 77-80 | 4 | 2 |
| α-helix | 92-103 | 12 | |
| α-helix | 107-120 | 14 | |
| α-helix | 131-133 | 3 | |
| α-helix | 136-149 | 14 | |
| β-strand | 154-158 | 5 | 2 |
| α-helix | 166-183 | 18 | |
| β-strand | 186-190 | 5 | 2 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-207 | 5 | 2 |
| β-strand | 212-216 | 5 | 2 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 3 |
| α-helix | 228-233 | 6 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240-249 | 10 | 4 |
| β-strand | 254-257 | 4 | 4 |
| α-helix | 258 | 1 | |
| β-strand | 265-268 | 4 | 4 |
| β-strand | 270 | 1 | 5 |
| β-strand | 280-285 | 6 | 4 |
| α-helix | 287-289 | 3 | |
| α-helix | 290 | 1 | |
| β-strand | 291-292 | 2 | 6 |
| β-strand | 299-309 | 11 | 6 |
| β-strand | 313-319 | 7 | 6 |
| β-strand | 326-332 | 7 | 6 |
| β-strand | 342-346 | 5 | 6 |
| α-helix | 349-351 | 3 | |
| β-strand | 352-355 | 4 | 4 |
| β-strand | 360 | 1 | 3 |
| β-strand | 361 | 1 | 4 |
| α-helix | 362-363 | 2 | |
| β-strand | 364 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-8 | 4 | 7 |
| β-strand | 9-13 | 5 | 8 |
| β-strand | 16-22 | 7 | 8 |
| β-strand | 25 | 1 | 7 |
| β-strand | 31-35 | 5 | 9 |
| α-helix | 42-50 | 9 | |
| β-strand | 57-62 | 6 | 7 |
| β-strand | 65-66 | 2 | 7 |
| β-strand | 77-79 | 3 | 9 |
| α-helix | 92-102 | 11 | |
| α-helix | 109-120 | 12 | |
| α-helix | 136-149 | 14 | |
| β-strand | 154-158 | 5 | 9 |
| α-helix | 166-183 | 18 | |
| β-strand | 186-190 | 5 | 9 |
| α-helix | 194-199 | 6 | |
| β-strand | 203-207 | 5 | 9 |
| β-strand | 212-216 | 5 | 9 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 10 |
| α-helix | 228-233 | 6 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240-249 | 10 | 11 |
| β-strand | 254-257 | 4 | 11 |
| β-strand | 265-268 | 4 | 11 |
| β-strand | 270 | 1 | 12 |
| α-helix | 275-276 | 2 | |
| β-strand | 280-285 | 6 | 11 |
| α-helix | 287-289 | 3 | |
| α-helix | 290 | 1 | |
| β-strand | 291-292 | 2 | 13 |
| β-strand | 302-309 | 8 | 14 |
| β-strand | 313-319 | 7 | 14 |
| β-strand | 327-332 | 6 | 14 |
| β-strand | 342-343 | 2 | 14 |
| β-strand | 345-346 | 2 | 13 |
| α-helix | 349-351 | 3 | |
| β-strand | 353-355 | 3 | 11 |
| β-strand | 360 | 1 | 10 |
| β-strand | 361-362 | 2 | 11 |
| α-helix | 363 | 1 | |
| β-strand | 364 | 1 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-36 | 18 | |
| α-helix | 40-58 | 19 | |
| α-helix | 63-75 | 13 | |
| α-helix | 76-80 | 5 | |
| α-helix | 81-89 | 9 | |
| α-helix | 262-268 | 7 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-307 | 34 | |
| α-helix | 314-322 | 9 | |
| α-helix | 323-325 | 3 | |
| α-helix | 332-339 | 8 | |
| α-helix | 365-392 | 28 | |
| α-helix | 397-405 | 9 | |
| α-helix | 410-413 | 4 | |
| α-helix | 414-418 | 5 | |
| α-helix | 419-438 | 20 | |
| β-strand | 449 | 1 | 15 |
| β-strand | 461 | 1 | 15 |
| α-helix | 478-482 | 5 | |
| α-helix | 484-502 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6 | 1 | |
| α-helix | 9-28 | 20 | |
| α-helix | 34-37 | 4 | |
| α-helix | 84-112 | 29 | |
| α-helix | 118-129 | 12 | |
| α-helix | 133-147 | 15 | |
| α-helix | 172-183 | 12 | |
| α-helix | 187-194 | 8 | |
| α-helix | 199-202 | 4 | |
| α-helix | 203-207 | 5 | |
| α-helix | 208-227 | 20 | |
| α-helix | 245-252 | 8 | |
| α-helix | 263-282 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin import ATP-binding protein MalK | A, B | protein | 371 | Escherichia coli K-12 | P68187 (AlphaFold model) |
| Maltose/maltodextrin transport system permease protein MalF | F | protein | 514 | Escherichia coli K-12 | P02916 (AlphaFold model) |
| Maltose/maltodextrin transport system permease protein MalG | G | protein | 296 | Escherichia coli K-12 | P68183 (AlphaFold model) |
>9NQJ_1 Maltose/maltodextrin import ATP-binding protein MalK (chains A, B) ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLF IGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVL QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHK RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILE GEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTA CRRLHKEPGVA
>9NQJ_2 Maltose/maltodextrin transport system permease protein MalF (chains F) MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANR KAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTY NFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNR QALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSI TADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGM VLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPA WFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLP LLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGG GQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD
>9NQJ_3 Maltose/maltodextrin transport system permease protein MalG (chains G) MAMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLIPEQISWDHWK LALGFSVEQADGRITPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKAT LLKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGY FETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDV NSYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVNGLTAGGVKG
| ID | Name | Formula | Copies |
|---|---|---|---|
| VO4 | Vanadate ion | O4 V | 2 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
| MG | Magnesium ion | Mg | 2 |
DeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides. Ren, Q., Wang, J., Idikuda, V. et al. Nat Commun (2025) 16:7973-7973. DOI 10.1038/s41467-025-63275-8 · PubMed
Other PDB entries of the same protein (UniProt P68187 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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