Crystal structure of the human telomeric Stn1-Ten1 complex. Determined by X-ray diffraction at 2.05 Å resolution. Released 29 May 2013.
Explore 4JOI in 3D Show helices and sheets RCSB PDB PDBe
4JOI contains 24 α-helices and 30 β-strands across 4 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 | 27-28 | 2 | 1 |
| α-helix | 31-36 | 6 | |
| α-helix | 37 | 1 | |
| β-strand | 38-39 | 2 | 2 |
| α-helix | 40 | 1 | |
| β-strand | 47-49 | 3 | 2 |
| β-strand | 52-54 | 3 | 2 |
| β-strand | 56-68 | 13 | 1 |
| β-strand | 72-78 | 7 | 1 |
| β-strand | 83-89 | 7 | 1 |
| α-helix | 113-118 | 6 | |
| α-helix | 119-122 | 4 | |
| β-strand | 131-141 | 11 | 1 |
| β-strand | 144-155 | 12 | 1 |
| α-helix | 161-173 | 13 | |
| α-helix | 174-178 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27-28 | 2 | 3 |
| α-helix | 31-36 | 6 | |
| α-helix | 37 | 1 | |
| β-strand | 38-39 | 2 | 4 |
| α-helix | 40 | 1 | |
| β-strand | 47-49 | 3 | 4 |
| β-strand | 52-54 | 3 | 4 |
| β-strand | 56-68 | 13 | 3 |
| β-strand | 72-78 | 7 | 3 |
| β-strand | 83-89 | 7 | 3 |
| α-helix | 116-120 | 5 | |
| α-helix | 121-123 | 3 | |
| β-strand | 131-141 | 11 | 3 |
| β-strand | 144-155 | 12 | 3 |
| α-helix | 161-173 | 13 | |
| α-helix | 174-178 | 5 | |
| α-helix | 181-182 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| β-strand | 8-9 | 2 | 6 |
| α-helix | 12-16 | 5 | |
| β-strand | 25-36 | 12 | 6 |
| β-strand | 41-47 | 7 | 6 |
| β-strand | 52-58 | 7 | 6 |
| β-strand | 72-80 | 9 | 6 |
| β-strand | 88-96 | 9 | 6 |
| α-helix | 102-118 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| β-strand | 8-9 | 2 | 5 |
| α-helix | 12-16 | 5 | |
| β-strand | 25-36 | 12 | 5 |
| β-strand | 41-48 | 8 | 5 |
| β-strand | 51-58 | 8 | 5 |
| α-helix | 60-62 | 3 | |
| α-helix | 63 | 1 | |
| α-helix | 65 | 1 | |
| β-strand | 72-80 | 9 | 5 |
| β-strand | 88-96 | 9 | 5 |
| α-helix | 102-118 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CST complex subunit STN1 | A, B | protein | 166 | Homo sapiens | Q9H668 (AlphaFold model) |
| CST complex subunit TEN1 | C, D | protein | 122 | Homo sapiens | Q86WV5 (AlphaFold model) |
>4JOI_1 CST complex subunit STN1 (chains A, B) LDPVFLAFAKLYIRDILDMKESRQVPGVFLYNGHPIKQVDVLGTVIGVRERDAFYSYGVD DSTGVINCICWKKLNTESVSAAPSAARELSLTSQLKKLQETIEQKTKIEIGDTIRVRGSI RTYREEREIHATTYYKVDDPVWNIQIARMLELPTIYRKVYDQPFHS
>4JOI_2 CST complex subunit TEN1 (chains C, D) MLPKPGTYYLPWEVSAGQVPDGSTLRTFGRLCLYDMIQSRVTLMAQHGSDQHQVLVCTKL VEPFHAQVGSLYIVLGELQHQQDRGSVVKARVLTCVEGMNLPLLEQAIREQRLYKQERGG SQ
Structure of the human telomeric stn1-ten1 capping complex. Bryan, C., Rice, C., Harkisheimer, M. et al. PLoS One (2013) 8:e66756-e66756. DOI 10.1371/journal.pone.0066756 · PubMed
Other PDB entries of the same protein (UniProt Q9H668 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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