Mycobacterium tuberculosis EmbR. Determined by X-ray diffraction at 2.0 Å resolution. Released 24 Jan 2006.
Explore 2FEZ in 3D Show helices and sheets RCSB PDB PDBe
2FEZ contains 18 α-helices and 20 β-strands across 1 chain. 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 | 11-14 | 4 | 1 |
| β-strand | 20-23 | 4 | 1 |
| β-strand | 26-27 | 2 | 1 |
| α-helix | 33-44 | 12 | |
| β-strand | 49-50 | 2 | 2 |
| α-helix | 52-60 | 9 | |
| α-helix | 68-83 | 16 | |
| α-helix | 84-86 | 3 | |
| α-helix | 90-93 | 4 | |
| β-strand | 94-97 | 4 | 2 |
| β-strand | 100-103 | 4 | 2 |
| α-helix | 107-109 | 3 | |
| β-strand | 110 | 1 | 1 |
| α-helix | 111-127 | 17 | |
| α-helix | 131-142 | 12 | |
| α-helix | 151-153 | 3 | |
| α-helix | 159-183 | 25 | |
| α-helix | 187-200 | 14 | |
| α-helix | 205-217 | 13 | |
| α-helix | 221-239 | 19 | |
| α-helix | 242-244 | 3 | |
| α-helix | 245-255 | 11 | |
| α-helix | 262-280 | 19 | |
| β-strand | 281 | 1 | 3 |
| β-strand | 287 | 1 | 3 |
| α-helix | 288-290 | 3 | |
| β-strand | 291-294 | 4 | 4 |
| β-strand | 300-302 | 3 | 4 |
| β-strand | 307-311 | 5 | 5 |
| β-strand | 318-319 | 2 | 5 |
| β-strand | 330-334 | 5 | 5 |
| β-strand | 339-343 | 5 | 5 |
| β-strand | 351-352 | 2 | 4 |
| β-strand | 355-356 | 2 | 4 |
| β-strand | 360-362 | 3 | 5 |
| α-helix | 363-364 | 2 | |
| β-strand | 368-371 | 4 | 4 |
| β-strand | 374-379 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Probable regulatory protein embR | A | protein | 388 | Mycobacterium tuberculosis | P9WGJ9 (AlphaFold model) |
>2FEZ_1 Probable regulatory protein embR (chains A) MAGSATVEKRLDFGLLGPLQMTIDGTPVPSGTPKQRAVLAMLVINRNRPVGVDALITALW EEWPPSGARASIHSYVSNLRKLLGGAGIDPRVVLAAAPPGYRLSIPDNTCDLGRFVAEKT AGVHAAAAGRFEQASRHLSAALREWRGPVLDDLRDFQFVEPFATALVEDKVLAHTAKAEA EIACGRASAVIAELEALTFEHPYREPLWTQLITAYYLSDRQSDALGAYRRVKTTLADDLG IDPGPTLRALNERILRQQPLDAKKSAKTTAAGTVTVLDQRTMASGQQAVAYLHDIASGRG YPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYVINDLRSSNGVHVQHERIRSA VTLNDGDHIRICDHEFTFQISAGTHGGT
Molecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis. Alderwick, L.J., Molle, V., Kremer, L. et al. Proc Natl Acad Sci U S A (2006) 103:2558-2563. DOI 10.1073/pnas.0507766103 · PubMed
Other PDB entries of the same protein (UniProt P9WGJ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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