The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form. Determined by X-ray diffraction at 2.9 Å resolution. Released 30 Sept 2003.
Explore 1Q1E in 3D Show helices and sheets RCSB PDB PDBe
1Q1E contains 30 α-helices and 48 β-strands across 2 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 | 5-13 | 9 | 1 |
| β-strand | 16-25 | 10 | 1 |
| β-strand | 31-35 | 5 | 2 |
| α-helix | 42-50 | 9 | |
| β-strand | 57-62 | 6 | 1 |
| β-strand | 65-66 | 2 | 1 |
| α-helix | 72-75 | 4 | |
| β-strand | 77-79 | 3 | 2 |
| α-helix | 92-102 | 11 | |
| α-helix | 107-120 | 14 | |
| α-helix | 131-133 | 3 | |
| α-helix | 136-148 | 13 | |
| β-strand | 154-157 | 4 | 2 |
| α-helix | 167-183 | 17 | |
| β-strand | 186-191 | 6 | 2 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-208 | 6 | 2 |
| β-strand | 211-216 | 6 | 2 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 3 |
| α-helix | 228-233 | 6 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240-248 | 9 | 4 |
| β-strand | 255-257 | 3 | 4 |
| β-strand | 265-267 | 3 | 4 |
| β-strand | 270 | 1 | 5 |
| β-strand | 280-285 | 6 | 4 |
| α-helix | 287-289 | 3 | |
| β-strand | 291 | 1 | 6 |
| β-strand | 299-309 | 11 | 6 |
| β-strand | 313-319 | 7 | 6 |
| α-helix | 326 | 1 | |
| β-strand | 327-332 | 6 | 6 |
| β-strand | 342-346 | 5 | 6 |
| α-helix | 349-351 | 3 | |
| β-strand | 353-355 | 3 | 4 |
| β-strand | 360 | 1 | 3 |
| β-strand | 361 | 1 | 4 |
| β-strand | 364 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-13 | 9 | 7 |
| β-strand | 16-25 | 10 | 7 |
| β-strand | 31-35 | 5 | 8 |
| α-helix | 42-50 | 9 | |
| β-strand | 57-62 | 6 | 7 |
| β-strand | 65-66 | 2 | 7 |
| α-helix | 72-74 | 3 | |
| β-strand | 77-79 | 3 | 8 |
| α-helix | 92-102 | 11 | |
| α-helix | 107-120 | 14 | |
| α-helix | 124-126 | 3 | |
| α-helix | 131-133 | 3 | |
| α-helix | 136-148 | 13 | |
| β-strand | 154-157 | 4 | 8 |
| α-helix | 167-183 | 17 | |
| β-strand | 186-191 | 6 | 8 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-208 | 6 | 8 |
| β-strand | 211-216 | 6 | 8 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 9 |
| α-helix | 228-231 | 4 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240-250 | 11 | 10 |
| β-strand | 253-257 | 5 | 10 |
| β-strand | 265-268 | 4 | 10 |
| β-strand | 280-285 | 6 | 10 |
| α-helix | 287-289 | 3 | |
| β-strand | 291 | 1 | 11 |
| β-strand | 298-309 | 12 | 11 |
| β-strand | 313-319 | 7 | 11 |
| α-helix | 326 | 1 | |
| β-strand | 327-332 | 6 | 11 |
| β-strand | 342-347 | 6 | 11 |
| α-helix | 349-351 | 3 | |
| β-strand | 353-355 | 3 | 10 |
| β-strand | 360 | 1 | 9 |
| β-strand | 361 | 1 | 10 |
| α-helix | 366-368 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin transport ATP-binding protein malK | A, B | protein | 381 | Escherichia coli | P68187 (AlphaFold model) |
>1Q1E_1 Maltose/maltodextrin transport ATP-binding protein malK (chains A, B) MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL FIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEV LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN FLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVIL EGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGT ACRRLHKEPGVASASHHHHHH
A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Chen, J., Lu, G., Lin, J. et al. Mol Cell (2003) 12:651-661. DOI 10.1016/j.molcel.2003.08.004 · 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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