Crystal structure of the inactive retinoblastoma protein phosphorylated at T373. Determined by X-ray diffraction at 2.7 Å resolution. Released 23 May 2012.
Explore 4ELJ in 3D Show helices and sheets RCSB PDB PDBe
4ELJ contains 41 α-helices and 6 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 |
|---|---|---|---|
| α-helix | 55-63 | 9 | |
| α-helix | 68-84 | 17 | |
| α-helix | 96-109 | 14 | |
| α-helix | 117-124 | 8 | |
| α-helix | 128-137 | 10 | |
| α-helix | 142-169 | 28 | |
| β-strand | 173 | 1 | 1 |
| α-helix | 187-205 | 19 | |
| α-helix | 212-229 | 18 | |
| α-helix | 232-234 | 3 | |
| β-strand | 235 | 1 | 1 |
| α-helix | 237-240 | 4 | |
| α-helix | 272-280 | 9 | |
| α-helix | 285-291 | 7 | |
| α-helix | 292-296 | 5 | |
| α-helix | 297-301 | 5 | |
| α-helix | 304-306 | 3 | |
| β-strand | 307-308 | 2 | 2 |
| β-strand | 311-312 | 2 | 2 |
| α-helix | 314-328 | 15 | |
| α-helix | 333-338 | 6 | |
| α-helix | 341-343 | 3 | |
| α-helix | 374-388 | 15 | |
| α-helix | 398-405 | 8 | |
| α-helix | 412-434 | 23 | |
| α-helix | 436-438 | 3 | |
| α-helix | 439-468 | 30 | |
| α-helix | 474-478 | 5 | |
| α-helix | 480-498 | 19 | |
| α-helix | 500-501 | 2 | |
| α-helix | 516-520 | 5 | |
| α-helix | 525-538 | 14 | |
| α-helix | 544-559 | 16 | |
| α-helix | 561-563 | 3 | |
| α-helix | 569-574 | 6 | |
| α-helix | 646-669 | 24 | |
| α-helix | 675-690 | 16 | |
| α-helix | 692-694 | 3 | |
| α-helix | 700-714 | 15 | |
| α-helix | 721-729 | 9 | |
| α-helix | 737-740 | 4 | |
| β-strand | 742-745 | 4 | 3 |
| β-strand | 748-750 | 3 | 3 |
| α-helix | 752-755 | 4 | |
| α-helix | 756-760 | 5 | |
| α-helix | 761-764 | 4 | |
| α-helix | 768-770 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoblastoma-associated protein | A | protein | 656 | Homo sapiens | P06400 (AlphaFold model) |
>4ELJ_1 Retinoblastoma-associated protein (chains A) GEFEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVD LDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTC ELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKL SPPMLLKEPYKTAVIENDTRIIEVLCKEHECNIDEVANVAFKNFIPFMNSLGLVTSNGLP EVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPH TPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAK AVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALE VVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLER CEHRIMESLAWLSDSPLFDLIKQSKDREGPLKSTSLSLFYKKVYRLAYLRLNTLCERLLS EHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDL PHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLAPIPHIPR
Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. Burke, J.R., Hura, G.L., Rubin, S.M. Genes Dev (2012) 26:1156-1166. DOI 10.1101/gad.189837.112 · PubMed
Other PDB entries of the same protein (UniProt P06400 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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