Crystal structure of a membrane protein. Determined by X-ray diffraction at 3.35 Å resolution. Released 31 Oct 2012.
Explore 3UDC in 3D Show helices and sheets RCSB PDB PDBe
3UDC contains 49 α-helices and 70 β-strands across 7 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 | 17-50 | 34 | |
| α-helix | 60-87 | 28 | |
| α-helix | 92-109 | 18 | |
| α-helix | 111-125 | 15 | |
| β-strand | 134-137 | 4 | 1 |
| β-strand | 140-147 | 8 | 1 |
| β-strand | 151-156 | 6 | 1 |
| β-strand | 160-165 | 6 | 1 |
| α-helix | 166-168 | 3 | |
| β-strand | 172-174 | 3 | 1 |
| β-strand | 180-189 | 10 | 2 |
| α-helix | 194-211 | 18 | |
| β-strand | 215 | 1 | 2 |
| β-strand | 220-228 | 9 | 2 |
| β-strand | 231-240 | 10 | 2 |
| α-helix | 245-262 | 18 | |
| β-strand | 273-278 | 6 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-50 | 34 | |
| α-helix | 60-87 | 28 | |
| α-helix | 92-109 | 18 | |
| α-helix | 111-125 | 15 | |
| β-strand | 134-137 | 4 | 1 |
| β-strand | 140-147 | 8 | 1 |
| β-strand | 151-156 | 6 | 1 |
| β-strand | 160-165 | 6 | 1 |
| α-helix | 166-168 | 3 | |
| β-strand | 172-174 | 3 | 1 |
| β-strand | 180-189 | 10 | 4 |
| α-helix | 194-211 | 18 | |
| β-strand | 215 | 1 | 4 |
| β-strand | 220-228 | 9 | 4 |
| β-strand | 231-240 | 10 | 4 |
| α-helix | 245-262 | 18 | |
| β-strand | 271-278 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-47 | 31 | |
| α-helix | 60-87 | 28 | |
| α-helix | 92-109 | 18 | |
| α-helix | 111-125 | 15 | |
| β-strand | 134-137 | 4 | 1 |
| β-strand | 140-147 | 8 | 1 |
| β-strand | 151-156 | 6 | 1 |
| β-strand | 160-165 | 6 | 1 |
| α-helix | 166-168 | 3 | |
| β-strand | 172-174 | 3 | 1 |
| β-strand | 180-189 | 10 | 5 |
| α-helix | 194-211 | 18 | |
| β-strand | 215 | 1 | 5 |
| β-strand | 220-228 | 9 | 5 |
| β-strand | 231-240 | 10 | 5 |
| α-helix | 245-262 | 18 | |
| β-strand | 273-278 | 6 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Small-conductance mechanosensitive channel, C-terminal peptide from Small-conductance… | A, B, C, D, E, F, G | protein | 285 | Thermoanaerobacter tengcongensis, Escherichia coli | P0C0S1 (AlphaFold model), Q8R6L9 (AlphaFold model) |
>3UDC_1 Small-conductance mechanosensitive channel, C-terminal peptide from Small-conductance mechanosensitive channel (chains A, B, C, D, E, F, G) MWADIYHKLVEIYDIKAVKFLLDVLKILIIAFIGIKFADFLIYRFYKLYSKSKIQLPQRK IDTLTSLTKNAVRYIIYFLAGASILKLFNIDMTSLLAVAGIGSLAIGFGAQNLVKDMISG FFIIFEDQFSVGDYVTINGISGTVEEIGLRVTKIRGFSDGLHIIPNGEIKMVTNLTKDSM MAVVNIAFPIDEDVDKIIEGLQEICEEVKKSRDDLIEGPTVLGITDMQDSKLVIMVYAKT QPMQKWAVERDIRYRVKKMFDQKNISFPYPQMDVNFKRVKEDKAA
Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance. Zhang, X., Wang, J., Feng, Y. et al. Proc Natl Acad Sci U S A (2012) 109:18180-18185. DOI 10.1073/pnas.1207977109 · PubMed
Other PDB entries of the same protein (UniProt P0C0S1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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