p107 pocket domain complexed with mutated HDAC1-3X peptide. Determined by X-ray diffraction at 3.0 Å resolution. Released 29 Jun 2022.
Explore 7SMF in 3D Show helices and sheets RCSB PDB PDBe
7SMF contains 46 α-helices and 6 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 |
|---|---|---|---|
| α-helix | 392-400 | 9 | |
| α-helix | 412-417 | 6 | |
| α-helix | 424-442 | 19 | |
| β-strand | 446 | 1 | 1 |
| β-strand | 449 | 1 | 1 |
| α-helix | 454-478 | 25 | |
| α-helix | 480-483 | 4 | |
| α-helix | 491-493 | 3 | |
| α-helix | 495-512 | 18 | |
| α-helix | 521-525 | 5 | |
| α-helix | 530-533 | 4 | |
| α-helix | 534-536 | 3 | |
| α-helix | 537-541 | 5 | |
| α-helix | 549-564 | 16 | |
| α-helix | 574-579 | 6 | |
| α-helix | 788-809 | 22 | |
| α-helix | 817-830 | 14 | |
| α-helix | 840-853 | 14 | |
| α-helix | 861-868 | 8 | |
| α-helix | 877-880 | 4 | |
| β-strand | 883 | 1 | 2 |
| β-strand | 927 | 1 | 2 |
| α-helix | 930-933 | 4 | |
| α-helix | 934-938 | 5 | |
| α-helix | 939-946 | 8 | |
| α-helix | 962-964 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 392-400 | 9 | |
| α-helix | 410-418 | 9 | |
| α-helix | 424-443 | 20 | |
| α-helix | 454-478 | 25 | |
| α-helix | 480-483 | 4 | |
| α-helix | 490-493 | 4 | |
| α-helix | 495-512 | 18 | |
| α-helix | 521-525 | 5 | |
| α-helix | 530-533 | 4 | |
| α-helix | 534-536 | 3 | |
| α-helix | 537-542 | 6 | |
| α-helix | 549-564 | 16 | |
| α-helix | 573-579 | 7 | |
| α-helix | 588-592 | 5 | |
| α-helix | 787-809 | 23 | |
| α-helix | 817-829 | 13 | |
| α-helix | 832-835 | 4 | |
| α-helix | 840-853 | 14 | |
| α-helix | 861-869 | 9 | |
| α-helix | 876-878 | 3 | |
| β-strand | 883 | 1 | 3 |
| β-strand | 927 | 1 | 3 |
| α-helix | 930-933 | 4 | |
| α-helix | 934-938 | 5 | |
| α-helix | 939-946 | 8 | |
| α-helix | 961-963 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoblastoma-like protein 1 | A, C | protein | 371 | Homo sapiens | P28749 (AlphaFold model) |
| Histone deacetylase 1 | B, D | protein | 10 | Homo sapiens |
>7SMF_1 Retinoblastoma-like protein 1 (chains A, C) GEFTQSVSRLQSIVAGLKNAPSDQLINIFESCVRNPVENIMKILKGIGETFCQHYTQSTD EQPGSHIDFAVNRLKLAEILYYKILETVMVQETRRLHGMDMSVLLEQDIFHRSLMACCLE IVLFAYSSPRTFPWIIEVLNLQPFYFYKVIEVVIRSEEGLSRDMVKHLNSIEEQILESLA WSHDSALWEALQVSANKVPTCEEVIFPNNFETGNNRPKRTGSLALFYRKVYHLASVRLRD LCLKLDVSNELRRKIWTCFEFTLVHCPDLMKDRHLDQLLLCAFYIMAKVTKEERTFQEIM KSYRNQPQANSHVYRSVLLKSIKEERGDLIKFYNTIYVGRVKSFALKYDLANQDHMMDAP PLSPFPHIKQQ
>7SMF_2 Histone deacetylase 1 (chains B, D) DIYCYEEFSD
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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