Structure of the tripartite motif of KAP1/TRIM28. Determined by X-ray diffraction at 2.9 Å resolution. Released 24 Jul 2019.
Explore 6QAJ in 3D Show helices and sheets RCSB PDB PDBe
6QAJ contains 41 α-helices and 36 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 | -101--97 | 5 | |
| β-strand | -93--92 | 2 | 1 |
| β-strand | -91 | 1 | 2 |
| β-strand | -90--88 | 3 | 1 |
| β-strand | -82--79 | 4 | 1 |
| β-strand | -76--73 | 4 | 1 |
| α-helix | -68--57 | 12 | |
| β-strand | -50 | 1 | 2 |
| α-helix | -47--27 | 21 | |
| α-helix | -22--18 | 5 | |
| α-helix | -14--1 | 14 | |
| α-helix | 1-4 | 4 | |
| α-helix | 8-15 | 8 | |
| α-helix | 19-26 | 8 | |
| α-helix | 30-34 | 5 | |
| α-helix | 36-48 | 13 | |
| α-helix | 52-60 | 9 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64 | 1 | 3 |
| β-strand | 71 | 1 | 3 |
| β-strand | 78-80 | 3 | 4 |
| β-strand | 86-88 | 3 | 4 |
| β-strand | 114-116 | 3 | 5 |
| β-strand | 123-125 | 3 | 5 |
| β-strand | 130 | 1 | 4 |
| α-helix | 207 | 1 | |
| β-strand | 208 | 1 | 6 |
| α-helix | 209 | 1 | |
| β-strand | 216 | 1 | 6 |
| β-strand | 219-221 | 3 | 7 |
| β-strand | 227-228 | 2 | 7 |
| α-helix | 230-235 | 6 | |
| β-strand | 242-243 | 2 | 7 |
| α-helix | 245-349 | 105 | |
| α-helix | 350-353 | 4 | |
| α-helix | 358-361 | 4 | |
| α-helix | 362-369 | 8 | |
| α-helix | 379-383 | 5 | |
| α-helix | 390-397 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -103--97 | 7 | |
| β-strand | -93--92 | 2 | 8 |
| β-strand | -91 | 1 | 9 |
| β-strand | -90--88 | 3 | 8 |
| β-strand | -82--79 | 4 | 8 |
| β-strand | -76--73 | 4 | 8 |
| α-helix | -68--57 | 12 | |
| β-strand | -50 | 1 | 9 |
| α-helix | -47--27 | 21 | |
| α-helix | -22--18 | 5 | |
| α-helix | -14--1 | 14 | |
| α-helix | 1-4 | 4 | |
| α-helix | 8-15 | 8 | |
| α-helix | 19-27 | 9 | |
| α-helix | 30-34 | 5 | |
| α-helix | 36-48 | 13 | |
| α-helix | 52-61 | 10 | |
| β-strand | 64 | 1 | 10 |
| β-strand | 71 | 1 | 10 |
| α-helix | 77-78 | 2 | |
| β-strand | 79-80 | 2 | 11 |
| β-strand | 86-87 | 2 | 11 |
| β-strand | 115-116 | 2 | 12 |
| β-strand | 123-124 | 2 | 12 |
| β-strand | 130 | 1 | 11 |
| α-helix | 207 | 1 | |
| β-strand | 208 | 1 | 13 |
| α-helix | 209 | 1 | |
| β-strand | 216 | 1 | 13 |
| β-strand | 217-220 | 4 | 14 |
| β-strand | 227-229 | 3 | 14 |
| α-helix | 230-235 | 6 | |
| β-strand | 244 | 1 | 14 |
| α-helix | 245-350 | 106 | |
| α-helix | 351-353 | 3 | |
| α-helix | 358-361 | 4 | |
| α-helix | 362-369 | 8 | |
| α-helix | 390-396 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endolysin,Transcription intermediary factor 1-beta | A, B | protein | 544 | Enterobacteria phage T4, Homo sapiens | P00720, Q13263 (AlphaFold model) |
>6QAJ_1 Endolysin,Transcription intermediary factor 1-beta (chains A, B) MGSSHHHHHHSQDPNSSSENLYFQGNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKS PSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRR CALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTG TWDAYAAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAA GDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVEC SEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTC RDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQK RVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFA SWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIV AERP
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 8 |
Structure of KAP1 tripartite motif identifies molecular interfaces required for retroelement silencing. Stoll, G.A., Oda, S.I., Chong, Z.S. et al. Proc Natl Acad Sci U S A (2019) 116:15042-15051. DOI 10.1073/pnas.1901318116 · PubMed
Other PDB entries of the same protein (UniProt P00720), best resolution first:
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