The crystal structure of human eEFSec in complex with GDPNP. Determined by X-ray diffraction at 3.4 Å resolution. Released 12 Oct 2016.
Explore 5IZM in 3D Show helices and sheets RCSB PDB PDBe
5IZM contains 24 α-helices and 77 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 |
|---|---|---|---|
| β-strand | 5-14 | 10 | 1 |
| α-helix | 20-29 | 10 | |
| β-strand | 52-59 | 8 | 1 |
| α-helix | 60-61 | 2 | |
| α-helix | 62-65 | 4 | |
| β-strand | 85-92 | 8 | 1 |
| α-helix | 97-99 | 3 | |
| α-helix | 100-106 | 7 | |
| β-strand | 112-118 | 7 | 1 |
| α-helix | 125-137 | 13 | |
| β-strand | 140-146 | 7 | 1 |
| α-helix | 156-172 | 17 | |
| β-strand | 181-183 | 3 | 1 |
| β-strand | 185 | 1 | 2 |
| β-strand | 200 | 1 | 2 |
| α-helix | 202-212 | 11 | |
| β-strand | 225-233 | 9 | 3 |
| β-strand | 239-247 | 9 | 3 |
| β-strand | 250-251 | 2 | 4 |
| β-strand | 255 | 1 | 5 |
| β-strand | 257 | 1 | 3 |
| β-strand | 266 | 1 | 5 |
| β-strand | 271 | 1 | 6 |
| β-strand | 276 | 1 | 6 |
| β-strand | 279-280 | 2 | 4 |
| β-strand | 285-286 | 2 | 3 |
| β-strand | 289-290 | 2 | 3 |
| β-strand | 301-304 | 4 | 3 |
| β-strand | 312-318 | 7 | 7 |
| β-strand | 320-321 | 2 | 7 |
| α-helix | 322 | 1 | |
| β-strand | 330 | 1 | 8 |
| β-strand | 335-340 | 6 | 7 |
| β-strand | 342-347 | 6 | 7 |
| β-strand | 350-353 | 4 | 7 |
| β-strand | 373-375 | 3 | 7 |
| β-strand | 378 | 1 | 8 |
| β-strand | 411-420 | 10 | 7 |
| β-strand | 427 | 1 | 9 |
| β-strand | 429-431 | 3 | 7 |
| β-strand | 444-447 | 4 | 7 |
| β-strand | 449 | 1 | 9 |
| β-strand | 452-454 | 3 | 7 |
| α-helix | 459-462 | 4 | |
| α-helix | 464-466 | 3 | |
| β-strand | 469-470 | 2 | 7 |
| β-strand | 487 | 1 | 10 |
| β-strand | 507 | 1 | 11 |
| β-strand | 510 | 1 | 12 |
| β-strand | 514 | 1 | 12 |
| β-strand | 517 | 1 | 11 |
| β-strand | 531 | 1 | 10 |
| β-strand | 582 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 13 |
| β-strand | 11-14 | 4 | 13 |
| α-helix | 20-30 | 11 | |
| β-strand | 52-59 | 8 | 13 |
| α-helix | 60-61 | 2 | |
| α-helix | 62-64 | 3 | |
| β-strand | 85-92 | 8 | 13 |
| α-helix | 97-99 | 3 | |
| α-helix | 100-105 | 6 | |
| β-strand | 112-118 | 7 | 13 |
| α-helix | 125-137 | 13 | |
| β-strand | 140-146 | 7 | 13 |
| α-helix | 157-170 | 14 | |
| β-strand | 181-183 | 3 | 13 |
| α-helix | 203-212 | 10 | |
| β-strand | 225-232 | 8 | 14 |
| β-strand | 239-247 | 9 | 14 |
| β-strand | 249-251 | 3 | 15 |
| β-strand | 255-258 | 4 | 14 |
| β-strand | 263-266 | 4 | 14 |
| β-strand | 269-272 | 4 | 14 |
| β-strand | 275-276 | 2 | 14 |
| β-strand | 279-281 | 3 | 15 |
| β-strand | 285 | 1 | 14 |
| β-strand | 287-290 | 4 | 14 |
| α-helix | 295-297 | 3 | |
| β-strand | 302-304 | 3 | 14 |
| β-strand | 310-321 | 12 | 16 |
| β-strand | 334-339 | 6 | 16 |
| β-strand | 342-353 | 12 | 16 |
| β-strand | 373-375 | 3 | 16 |
| β-strand | 411-422 | 12 | 16 |
| β-strand | 427-430 | 4 | 16 |
| β-strand | 446-454 | 9 | 16 |
| α-helix | 459-462 | 4 | |
| α-helix | 464-466 | 3 | |
| β-strand | 469-471 | 3 | 16 |
| β-strand | 474-476 | 3 | 17 |
| β-strand | 478-479 | 2 | 18 |
| β-strand | 487 | 1 | 17 |
| β-strand | 490-491 | 2 | 18 |
| α-helix | 500-503 | 4 | |
| β-strand | 507-510 | 4 | 17 |
| β-strand | 514-518 | 5 | 17 |
| β-strand | 530-531 | 2 | 17 |
| α-helix | 538-543 | 6 | |
| β-strand | 575-578 | 4 | 17 |
| β-strand | 581-582 | 2 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Selenocysteine-specific elongation factor | A, B | protein | 616 | Homo sapiens | P57772 (AlphaFold model) |
>5IZM_1 Selenocysteine-specific elongation factor (chains A, B) MGSSHHHHHHSSGLVPRGSHMAGRRVNVNVGVLGHIDSGKTALARALSTTASTAAFDKQP QSRERGITLDLGFSCFSVPLPARLRSSLPEFQAAPEAEPEPGEPLLQVTLVDCPGHASLI RTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLPEGKRQAAI DKMTKKMQKTLENTKFRGAPIIPVAAKPGGPEAPETEAPQGIPELIELLTSQISIPTRDP SGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSA MQGDRLGICVTQFDPKLLERGLVCAPESLHTVHAALISVEKIPYFRGPLQTKAKFHITVG HETVMGRLMFFSPAPDNFDQEPILDSFNFSQEYLFQEQYLSKDLTPAVTDNDEADKKAGQ ATEGHCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGILLHGLEDRNYA DSFLPRLKVYKLKHKHGLVERAMDDYSVIGRSLFKKETNIQLFVGLKVHLSTGELGIIDS AFGQSGKFKIHIPGGLSPESKKILTPALKKRARAGRGEATRQEESAERSEPSQHVVLSLT FKRYVFDTHKRMVQSP
| ID | Name | Formula | Copies |
|---|---|---|---|
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 2 |
| MN | Manganese (II) ion | Mn | 2 |
Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation. Dobosz-Bartoszek, M., Pinkerton, M.H., Otwinowski, Z. et al. Nat Commun (2016) 7:12941-12941. DOI 10.1038/ncomms12941 · PubMed
Other PDB entries of the same protein (UniProt P57772 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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