Cryo-EM structure of E.coli MlaFEB. Determined by electron microscopy at 3.9 Å resolution. Released 19 May 2021.
Explore 7CH7 in 3D Show helices and sheets RCSB PDB PDBe
7CH7 contains 63 α-helices and 34 β-strands across 6 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 |
|---|---|---|---|
| α-helix | 14-18 | 5 | |
| α-helix | 19-28 | 10 | |
| α-helix | 40-47 | 8 | |
| α-helix | 48-54 | 7 | |
| α-helix | 56-78 | 23 | |
| α-helix | 87-94 | 8 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-111 | 12 | |
| α-helix | 117-126 | 10 | |
| α-helix | 128-134 | 7 | |
| α-helix | 139 | 1 | |
| α-helix | 140-144 | 5 | |
| α-helix | 145-171 | 27 | |
| α-helix | 172-177 | 6 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-223 | 28 | |
| α-helix | 231-258 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-18 | 5 | |
| α-helix | 19-28 | 10 | |
| α-helix | 40-47 | 8 | |
| α-helix | 48-54 | 7 | |
| α-helix | 56-78 | 23 | |
| α-helix | 87-97 | 11 | |
| α-helix | 100-111 | 12 | |
| α-helix | 117-126 | 10 | |
| α-helix | 128-134 | 7 | |
| α-helix | 139 | 1 | |
| α-helix | 140-144 | 5 | |
| α-helix | 145-171 | 27 | |
| α-helix | 172-177 | 6 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-223 | 28 | |
| α-helix | 231-258 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-14 | 8 | 1 |
| β-strand | 15 | 1 | 2 |
| β-strand | 27-32 | 6 | 1 |
| β-strand | 37-40 | 4 | 3 |
| α-helix | 47-54 | 8 | |
| β-strand | 62 | 1 | 2 |
| β-strand | 65-67 | 3 | 1 |
| β-strand | 71 | 1 | 1 |
| α-helix | 79-84 | 6 | |
| β-strand | 90-91 | 2 | 3 |
| α-helix | 102-113 | 12 | |
| α-helix | 118-132 | 15 | |
| α-helix | 135-137 | 3 | |
| α-helix | 147-159 | 13 | |
| β-strand | 167-169 | 3 | 3 |
| α-helix | 177-191 | 15 | |
| β-strand | 199-202 | 4 | 3 |
| α-helix | 205-208 | 4 | |
| β-strand | 215-219 | 5 | 3 |
| β-strand | 222-227 | 6 | 3 |
| α-helix | 229-233 | 5 | |
| α-helix | 238-245 | 8 | |
| α-helix | 256-257 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 7 |
| β-strand | 13-18 | 6 | 7 |
| α-helix | 26-29 | 4 | |
| α-helix | 32-35 | 4 | |
| β-strand | 41-43 | 3 | 7 |
| β-strand | 47 | 1 | 7 |
| α-helix | 52-65 | 14 | |
| β-strand | 74-75 | 2 | 7 |
| α-helix | 79-87 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lipid asymmetry maintenance ABC transporter permease subunit MlaE | A, B | protein | 260 | Escherichia coli (strain K12) | P64606 (AlphaFold model) |
| Phospholipid ABC transporter ATP-binding protein MlaF | C, D | protein | 269 | Escherichia coli (strain K12) | P63386 (AlphaFold model) |
| Lipid asymmetry maintenance protein MlaB | E, F | protein | 97 | Escherichia coli (strain K12) | P64602 (AlphaFold model) |
>7CH7_1 Lipid asymmetry maintenance ABC transporter permease subunit MlaE (chains A, B) MLLNALASLGHKGIKTLRTFGRAGLMLFNALVGKPEFRKHAPLLVRQLYNVGVLSMLIIV VSGVFIGMVLGLQGYLVLTTYSAETSLGMLVALSLLRELGPVVAALLFAGRAGSALTAEI GLMRATEQLSSMEMMAVDPLRRVISPRFWAGVISLPLLTVIFVAVGIWGGSLVGVSWKGI DSGFFWSAMQNAVDWRMDLVNCLIKSVVFAITVTWISLFNGYDAIPTSAGISRATTRTVV HSSLAVLGLDFVLTALMFGN
>7CH7_2 Phospholipid ABC transporter ATP-binding protein MlaF (chains C, D) MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP DHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPL LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRV RQFLDGIADGPVPFRYPAGDYHADLLPGS
>7CH7_3 Lipid asymmetry maintenance protein MlaB (chains E, F) MSESLSWMQTGDTLALSGELDQDVLLPLWEMREEAVKGITCIDLSRVSRVDTGGLALLLH LIDLAKKQGNNVTLQGVNDKVYTLAKLYNLPADVLPR
Structural Insight into Phospholipid Transport by the MlaFEBD Complex from P. aeruginosa. Zhou, C., Shi, H., Zhang, M. et al. J Mol Biol (2021) 433:166986-166986. DOI 10.1016/j.jmb.2021.166986 · PubMed
Other PDB entries of the same protein (UniProt P64606 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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