3UDC: Membrane protein

Crystal structure of a membrane protein. Determined by X-ray diffraction at 3.35 Å resolution. Released 31 Oct 2012.

Method
X-ray diffraction
Resolution
3.35 Å
Organisms
Thermoanaerobacter tengcongensis, Escherichia coli
Chains
7
Atoms
14,903
Mol. weight
227.24 kDa
Released
31 Oct 2012

Explore 3UDC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A, E and F: 7 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix17-5034
α-helix60-8728
α-helix92-10918
α-helix111-12515
β-strand134-13741
β-strand140-14781
β-strand151-15661
β-strand160-16561
α-helix166-1683
β-strand172-17431
β-strand180-189102
α-helix194-21118
β-strand21512
β-strand220-22892
β-strand231-240102
α-helix245-26218
β-strand273-27863
Chain B: 7 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix17-5034
α-helix60-8728
α-helix92-10918
α-helix111-12515
β-strand134-13741
β-strand140-14781
β-strand151-15661
β-strand160-16561
α-helix166-1683
β-strand172-17431
β-strand180-189104
α-helix194-21118
β-strand21514
β-strand220-22894
β-strand231-240104
α-helix245-26218
β-strand271-27883
Chains C, D and G: 7 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix17-4731
α-helix60-8728
α-helix92-10918
α-helix111-12515
β-strand134-13741
β-strand140-14781
β-strand151-15661
β-strand160-16561
α-helix166-1683
β-strand172-17431
β-strand180-189105
α-helix194-21118
β-strand21515
β-strand220-22895
β-strand231-240105
α-helix245-26218
β-strand273-27863

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Small-conductance mechanosensitive channel, C-terminal peptide from Small-conductance…A, B, C, D, E, F, Gprotein285Thermoanaerobacter tengcongensis, Escherichia coliP0C0S1 (AlphaFold model), Q8R6L9 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>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

Primary citation

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:

Browse structure collections

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