Lipoprotein-releasing system transmembrane protein LolC. Determined by X-ray diffraction at 1.88 Å resolution. Released 15 Nov 2017.
Explore 5NAA in 3D Show helices and sheets RCSB PDB PDBe
5NAA contains 26 α-helices and 26 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 |
|---|---|---|---|
| α-helix | 51-58 | 8 | |
| α-helix | 60-62 | 3 | |
| β-strand | 66-70 | 5 | 1 |
| β-strand | 75 | 1 | 2 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-96 | 7 | 1 |
| β-strand | 97-104 | 8 | 3 |
| β-strand | 109-117 | 9 | 3 |
| α-helix | 126-128 | 3 | |
| β-strand | 129-130 | 2 | 3 |
| α-helix | 134-136 | 3 | |
| β-strand | 143-147 | 5 | 3 |
| α-helix | 148-154 | 7 | |
| β-strand | 161-171 | 11 | 3 |
| β-strand | 178-190 | 13 | 3 |
| α-helix | 195-198 | 4 | |
| β-strand | 200-204 | 5 | 3 |
| α-helix | 205-211 | 7 | |
| α-helix | 214-215 | 2 | |
| β-strand | 219 | 1 | 2 |
| β-strand | 221-226 | 6 | 1 |
| α-helix | 229-231 | 3 | |
| α-helix | 232-235 | 4 | |
| β-strand | 244-248 | 5 | 1 |
| α-helix | 249-251 | 3 | |
| α-helix | 254-270 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 51-54 | 4 | |
| α-helix | 55-59 | 5 | |
| β-strand | 66-70 | 5 | 4 |
| β-strand | 75 | 1 | 5 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-96 | 7 | 4 |
| β-strand | 97-104 | 8 | 6 |
| β-strand | 109-117 | 9 | 6 |
| α-helix | 126-128 | 3 | |
| β-strand | 129-130 | 2 | 6 |
| α-helix | 134-136 | 3 | |
| β-strand | 143-147 | 5 | 6 |
| α-helix | 148-154 | 7 | |
| β-strand | 161-171 | 11 | 6 |
| β-strand | 178-190 | 13 | 6 |
| α-helix | 195-198 | 4 | |
| β-strand | 200-204 | 5 | 6 |
| α-helix | 205-211 | 7 | |
| α-helix | 214-215 | 2 | |
| β-strand | 219 | 1 | 5 |
| β-strand | 221-226 | 6 | 4 |
| α-helix | 229-231 | 3 | |
| α-helix | 232-235 | 4 | |
| β-strand | 244-248 | 5 | 4 |
| α-helix | 249-251 | 3 | |
| α-helix | 254-263 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lipoprotein-releasing system transmembrane protein LolC | A, B | protein | 230 | Escherichia coli | P0ADC3 (AlphaFold model) |
>5NAA_1 Lipoprotein-releasing system transmembrane protein LolC (chains A, B) MNGFERELQNNILGLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSAR SVAVGVMLGIDPAQKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVP SASQFTPMGRIPSQRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLD EPLKVDSLSQQKLPEGSKWQDWRDRKGELFQAVRMEKNMAAALEHHHHHH
Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily. Crow, A., Greene, N.P., Kaplan, E. et al. Proc Natl Acad Sci U S A (2017) 114:12572-12577. DOI 10.1073/pnas.1712153114 · PubMed
Other PDB entries of the same protein (UniProt P0ADC3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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