The crystal structure of human eEFSec in complex with GDP. Determined by X-ray diffraction at 3.25 Å resolution. Released 12 Oct 2016.
Explore 5IZK in 3D Show helices and sheets RCSB PDB PDBe
5IZK contains 18 α-helices and 75 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 | 6-13 | 8 | 1 |
| α-helix | 20-29 | 10 | |
| β-strand | 54 | 1 | 1 |
| β-strand | 57 | 1 | 1 |
| β-strand | 86-91 | 6 | 1 |
| α-helix | 97-104 | 8 | |
| α-helix | 107-109 | 3 | |
| β-strand | 110-118 | 9 | 1 |
| α-helix | 126-137 | 12 | |
| β-strand | 141-146 | 6 | 1 |
| α-helix | 153-171 | 19 | |
| β-strand | 181-183 | 3 | 1 |
| α-helix | 202-212 | 11 | |
| β-strand | 225-230 | 6 | 2 |
| β-strand | 242-247 | 6 | 2 |
| β-strand | 255-257 | 3 | 2 |
| β-strand | 264-271 | 8 | 2 |
| β-strand | 287-290 | 4 | 2 |
| β-strand | 302-304 | 3 | 2 |
| β-strand | 310-319 | 10 | 3 |
| β-strand | 321 | 1 | 4 |
| β-strand | 330 | 1 | 5 |
| β-strand | 337-338 | 2 | 6 |
| β-strand | 343-344 | 2 | 6 |
| β-strand | 346-347 | 2 | 3 |
| β-strand | 350-352 | 3 | 3 |
| α-helix | 360-362 | 3 | |
| β-strand | 373-376 | 4 | 3 |
| β-strand | 378 | 1 | 5 |
| β-strand | 410-422 | 13 | 3 |
| β-strand | 427-428 | 2 | 3 |
| β-strand | 429-430 | 2 | 6 |
| β-strand | 446 | 1 | 4 |
| β-strand | 448-454 | 7 | 3 |
| β-strand | 469-470 | 2 | 3 |
| β-strand | 473-478 | 6 | 7 |
| β-strand | 479 | 1 | 8 |
| β-strand | 484 | 1 | 9 |
| β-strand | 487 | 1 | 9 |
| β-strand | 488 | 1 | 10 |
| β-strand | 490 | 1 | 8 |
| β-strand | 507-510 | 4 | 7 |
| β-strand | 515-517 | 3 | 7 |
| β-strand | 518 | 1 | 10 |
| β-strand | 530 | 1 | 10 |
| α-helix | 538-542 | 5 | |
| β-strand | 574-579 | 6 | 7 |
| β-strand | 582 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-14 | 8 | 11 |
| α-helix | 21-29 | 9 | |
| β-strand | 87-91 | 5 | 11 |
| α-helix | 96-105 | 10 | |
| α-helix | 106-109 | 4 | |
| β-strand | 112-118 | 7 | 11 |
| α-helix | 125-137 | 13 | |
| β-strand | 141-146 | 6 | 11 |
| α-helix | 155-170 | 16 | |
| β-strand | 181-183 | 3 | 11 |
| α-helix | 204-209 | 6 | |
| α-helix | 210-212 | 3 | |
| β-strand | 225-227 | 3 | 12 |
| β-strand | 242-247 | 6 | 12 |
| β-strand | 255-258 | 4 | 12 |
| β-strand | 263-271 | 9 | 12 |
| β-strand | 285-290 | 6 | 12 |
| β-strand | 302-304 | 3 | 12 |
| β-strand | 310-311 | 2 | 13 |
| β-strand | 314-319 | 6 | 14 |
| β-strand | 321 | 1 | 15 |
| β-strand | 330 | 1 | 16 |
| β-strand | 336-338 | 3 | 15 |
| β-strand | 343-345 | 3 | 15 |
| β-strand | 349-351 | 3 | 14 |
| β-strand | 352 | 1 | 17 |
| α-helix | 357-359 | 3 | |
| β-strand | 372-374 | 3 | 17 |
| β-strand | 378 | 1 | 16 |
| β-strand | 410-415 | 6 | 14 |
| β-strand | 421-422 | 2 | 13 |
| β-strand | 428-430 | 3 | 15 |
| β-strand | 446-448 | 3 | 15 |
| β-strand | 450-453 | 4 | 14 |
| α-helix | 464-466 | 3 | |
| β-strand | 468-470 | 3 | 17 |
| β-strand | 474-479 | 6 | 18 |
| β-strand | 487-488 | 2 | 18 |
| β-strand | 490-491 | 2 | 18 |
| β-strand | 507-510 | 4 | 18 |
| β-strand | 515-518 | 4 | 18 |
| β-strand | 530-531 | 2 | 18 |
| α-helix | 541-543 | 3 | |
| β-strand | 574-578 | 5 | 18 |
| β-strand | 582 | 1 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Selenocysteine-specific elongation factor | A, B | protein | 616 | Homo sapiens | P57772 (AlphaFold model) |
>5IZK_1 Selenocysteine-specific elongation factor (chains A, B) MGSSHHHHHHSSGLVPRGSHMAGRRVNVNVGVLGHIDSGKTALARALSTTASTAAFDKQP QSRERGITLDLGFSCFSVPLPARLRSSLPEFQAAPEAEPEPGEPLLQVTLVDCPGHASLI RTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLPEGKRQAAI DKMTKKMQKTLENTKFRGAPIIPVAAKPGGPEAPETEAPQGIPELIELLTSQISIPTRDP SGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSA MQGDRLGICVTQFDPKLLERGLVCAPESLHTVHAALISVEKIPYFRGPLQTKAKFHITVG HETVMGRLMFFSPAPDNFDQEPILDSFNFSQEYLFQEQYLSKDLTPAVTDNDEADKKAGQ ATEGHCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGILLHGLEDRNYA DSFLPRLKVYKLKHKHGLVERAMDDYSVIGRSLFKKETNIQLFVGLKVHLSTGELGIIDS AFGQSGKFKIHIPGGLSPESKKILTPALKKRARAGRGEATRQEESAERSEPSQHVVLSLT FKRYVFDTHKRMVQSP
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 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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