Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2. Determined by electron microscopy at 3.51 Å resolution. Released 24 Sept 2025.
Explore 9NXC in 3D Show helices and sheets RCSB PDB PDBe
9NXC contains 69 α-helices and 56 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 | 7-8 | 2 | 4 |
| β-strand | 9-13 | 5 | 5 |
| β-strand | 16-22 | 7 | 5 |
| β-strand | 31-35 | 5 | 6 |
| α-helix | 39-50 | 12 | |
| β-strand | 57-59 | 3 | 4 |
| β-strand | 61-62 | 2 | 7 |
| β-strand | 65-66 | 2 | 7 |
| α-helix | 72-75 | 4 | |
| β-strand | 77-80 | 4 | 6 |
| α-helix | 92-96 | 5 | |
| α-helix | 98-102 | 5 | |
| α-helix | 109-119 | 11 | |
| α-helix | 124-126 | 3 | |
| α-helix | 131-133 | 3 | |
| α-helix | 136-150 | 15 | |
| β-strand | 154-157 | 4 | 6 |
| α-helix | 160-162 | 3 | |
| α-helix | 166-183 | 18 | |
| β-strand | 186-191 | 6 | 6 |
| α-helix | 194-199 | 6 | |
| β-strand | 203-208 | 6 | 6 |
| β-strand | 211-216 | 6 | 6 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 8 |
| α-helix | 228-233 | 6 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240-249 | 10 | 9 |
| β-strand | 253-257 | 5 | 9 |
| β-strand | 265-269 | 5 | 9 |
| β-strand | 280-285 | 6 | 9 |
| β-strand | 291-292 | 2 | 10 |
| β-strand | 299-309 | 11 | 10 |
| β-strand | 313-319 | 7 | 10 |
| β-strand | 326-332 | 7 | 10 |
| β-strand | 342-346 | 5 | 10 |
| α-helix | 349-351 | 3 | |
| β-strand | 353-355 | 3 | 9 |
| β-strand | 360 | 1 | 8 |
| β-strand | 361 | 1 | 9 |
| α-helix | 362-364 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-13 | 10 | 11 |
| β-strand | 16-26 | 11 | 11 |
| β-strand | 31-35 | 5 | 12 |
| α-helix | 41-50 | 10 | |
| β-strand | 57-62 | 6 | 11 |
| β-strand | 66 | 1 | 11 |
| β-strand | 77-80 | 4 | 12 |
| α-helix | 92-96 | 5 | |
| α-helix | 98-103 | 6 | |
| α-helix | 107-121 | 15 | |
| α-helix | 136-150 | 15 | |
| β-strand | 154-158 | 5 | 12 |
| α-helix | 160-162 | 3 | |
| α-helix | 166-183 | 18 | |
| β-strand | 186-190 | 5 | 12 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-207 | 5 | 12 |
| β-strand | 212-216 | 5 | 12 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 13 |
| α-helix | 228-233 | 6 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240-249 | 10 | 14 |
| β-strand | 254-257 | 4 | 14 |
| β-strand | 265-268 | 4 | 14 |
| β-strand | 270 | 1 | 15 |
| α-helix | 275-276 | 2 | |
| β-strand | 280-285 | 6 | 14 |
| α-helix | 290 | 1 | |
| β-strand | 291-292 | 2 | 16 |
| β-strand | 299-309 | 11 | 16 |
| β-strand | 313-319 | 7 | 16 |
| α-helix | 326 | 1 | |
| β-strand | 327-332 | 6 | 16 |
| β-strand | 342-346 | 5 | 16 |
| β-strand | 353-355 | 3 | 14 |
| β-strand | 360 | 1 | 13 |
| β-strand | 361-362 | 2 | 14 |
| α-helix | 363 | 1 | |
| β-strand | 364 | 1 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42-50 | 9 | |
| α-helix | 61-78 | 18 | |
| α-helix | 80-91 | 12 | |
| β-strand | 92 | 1 | 1 |
| α-helix | 252-254 | 3 | |
| β-strand | 258 | 1 | 1 |
| α-helix | 262-266 | 5 | |
| α-helix | 274-306 | 33 | |
| α-helix | 314-326 | 13 | |
| α-helix | 329-339 | 11 | |
| α-helix | 347-354 | 8 | |
| α-helix | 365-394 | 30 | |
| α-helix | 398-406 | 9 | |
| α-helix | 410-413 | 4 | |
| α-helix | 414-418 | 5 | |
| α-helix | 420-438 | 19 | |
| α-helix | 441-446 | 6 | |
| β-strand | 453 | 1 | 2 |
| β-strand | 462 | 1 | 2 |
| α-helix | 467-476 | 10 | |
| α-helix | 478-480 | 3 | |
| α-helix | 484-487 | 4 | |
| α-helix | 490-508 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-39 | 32 | |
| α-helix | 57-63 | 7 | |
| α-helix | 81-111 | 31 | |
| α-helix | 118-129 | 12 | |
| α-helix | 136-148 | 13 | |
| α-helix | 152-154 | 3 | |
| α-helix | 159-166 | 8 | |
| α-helix | 167-169 | 3 | |
| α-helix | 170-183 | 14 | |
| α-helix | 188-195 | 8 | |
| α-helix | 199-201 | 3 | |
| α-helix | 202-207 | 6 | |
| α-helix | 209-211 | 3 | |
| α-helix | 212-227 | 16 | |
| α-helix | 231-236 | 6 | |
| α-helix | 248-252 | 5 | |
| β-strand | 253-254 | 2 | 3 |
| β-strand | 257-258 | 2 | 3 |
| α-helix | 260-269 | 10 | |
| α-helix | 271-276 | 6 | |
| α-helix | 277-281 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin transport system permease protein MalF | H | protein | 519 | Escherichia coli | Q8FB38 (AlphaFold model) |
| Maltose/maltodextrin transport system permease protein MalG | I | protein | 286 | Escherichia coli | P68183 (AlphaFold model) |
| Maltose/maltodextrin import ATP-binding protein MalK | C | protein | 371 | Escherichia coli | P68187 (AlphaFold model) |
| Maltose/maltodextrin import ATP-binding protein MalK | D | protein | 373 | Escherichia coli | P68187 (AlphaFold model) |
>9NXC_1 Maltose/maltodextrin transport system permease protein MalF (chains H) MRKNPMDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLY IFANRKAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQ AGKIYNFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKESATQPEGERANLRV ITQNRQALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIG FYQSITADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLT VAVGMVLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALF GVKPAWFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFF KITLPLLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIA FEGGGGQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD
>9NXC_2 Maltose/maltodextrin transport system permease protein MalG (chains I) AMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLWPEQISWDHWKL ALGFSVEQADGRIWPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKATL LKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGYF ETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDVN SYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVN
>9NXC_3 Maltose/maltodextrin import ATP-binding protein MalK (chains C) ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLF IGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVL QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHK RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILE GEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTA CRRLHKEPGVA
>9NXC_4 Maltose/maltodextrin import ATP-binding protein MalK (chains D) ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLF IGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVL QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHK RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILE GEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTA CRRLHKEPGVAHH
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
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