p107 pocket domain complexed with EID1 peptide. Determined by X-ray diffraction at 2.15 Å resolution. Released 29 Jun 2022.
Explore 7SMD in 3D Show helices and sheets RCSB PDB PDBe
7SMD contains 25 α-helices and 2 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 | 392-401 | 10 | |
| α-helix | 410-418 | 9 | |
| α-helix | 424-442 | 19 | |
| α-helix | 454-478 | 25 | |
| α-helix | 480-483 | 4 | |
| α-helix | 489-492 | 4 | |
| α-helix | 495-512 | 18 | |
| α-helix | 521-525 | 5 | |
| α-helix | 530-533 | 4 | |
| α-helix | 535-543 | 9 | |
| α-helix | 549-564 | 16 | |
| α-helix | 566-568 | 3 | |
| α-helix | 574-580 | 7 | |
| α-helix | 585-587 | 3 | |
| α-helix | 588-592 | 5 | |
| α-helix | 787-809 | 23 | |
| α-helix | 814-830 | 17 | |
| α-helix | 832-835 | 4 | |
| α-helix | 840-855 | 16 | |
| α-helix | 861-868 | 8 | |
| α-helix | 877-880 | 4 | |
| β-strand | 882-885 | 4 | 1 |
| β-strand | 926-928 | 3 | 1 |
| α-helix | 930-933 | 4 | |
| α-helix | 934-938 | 5 | |
| α-helix | 939-946 | 8 | |
| α-helix | 947-949 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoblastoma-like protein 1 | A | protein | 371 | Homo sapiens | P28749 (AlphaFold model) |
| EP300-interacting inhibitor of differentiation 1 | B | protein | 14 | Homo sapiens | Q9Y6B2 (AlphaFold model) |
>7SMD_1 Retinoblastoma-like protein 1 (chains A) GEFTQSVSRLQSIVAGLKNAPSDQLINIFESCVRNPVENIMKILKGIGETFCQHYTQSTD EQPGSHIDFAVNRLKLAEILYYKILETVMVQETRRLHGMDMSVLLEQDIFHRSLMACCLE IVLFAYSSPRTFPWIIEVLNLQPFYFYKVIEVVIRSEEGLSRDMVKHLNSIEEQILESLA WSHDSALWEALQVSANKVPTCEEVIFPNNFETGNNRPKRTGSLALFYRKVYHLASVRLRD LCLKLDVSNELRRKIWTCFEFTLVHCPDLMKDRHLDQLLLCAFYIMAKVTKEERTFQEIM KSYRNQPQANSHVYRSVLLKSIKEERGDLIKFYNTIYVGRVKSFALKYDLANQDHMMDAP PLSPFPHIKQQ
>7SMD_2 EP300-interacting inhibitor of differentiation 1 (chains B) LTEELGCDEIIDRE
Structural basis for tunable affinity and specificity of LxCxE-dependent protein interactions with the retinoblastoma protein family. Putta, S., Alvarez, L., Ludtke, S. et al. Structure (2022) 30:1340. DOI 10.1016/j.str.2022.05.019 · PubMed
Other PDB entries of the same protein (UniProt P28749 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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