Crystal structure of the C-terminal region of yeast Ctf4, selenomethionine protein. Determined by X-ray diffraction at 2.69 Å resolution. Released 30 Apr 2014.
Explore 4C8H in 3D Show helices and sheets RCSB PDB PDBe
4C8H contains 33 α-helices and 74 β-strands across 3 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 | 479 | 1 | 1 |
| β-strand | 491-496 | 6 | 2 |
| β-strand | 500-507 | 8 | 2 |
| β-strand | 510-517 | 8 | 2 |
| β-strand | 526-530 | 5 | 2 |
| β-strand | 536-539 | 4 | 3 |
| β-strand | 543-547 | 5 | 3 |
| β-strand | 553-558 | 6 | 3 |
| α-helix | 564-565 | 2 | |
| β-strand | 566-569 | 4 | 3 |
| β-strand | 578-583 | 6 | 1 |
| β-strand | 588-592 | 5 | 1 |
| β-strand | 596-600 | 5 | 1 |
| β-strand | 606-611 | 6 | 1 |
| β-strand | 615-621 | 7 | 4 |
| β-strand | 624-631 | 8 | 4 |
| β-strand | 635-642 | 8 | 4 |
| β-strand | 649-656 | 8 | 4 |
| α-helix | 660-662 | 3 | |
| α-helix | 666-669 | 4 | |
| α-helix | 674-679 | 6 | |
| β-strand | 686-689 | 4 | 5 |
| β-strand | 695-698 | 4 | 5 |
| β-strand | 703-708 | 6 | 5 |
| β-strand | 717-723 | 7 | 5 |
| α-helix | 724-731 | 8 | |
| β-strand | 740-748 | 9 | 6 |
| β-strand | 751-758 | 8 | 6 |
| α-helix | 768 | 1 | |
| β-strand | 772-775 | 4 | 6 |
| β-strand | 777 | 1 | 5 |
| α-helix | 783-795 | 13 | |
| α-helix | 819-844 | 26 | |
| α-helix | 851-874 | 24 | |
| α-helix | 879-886 | 8 | |
| α-helix | 892-904 | 13 | |
| α-helix | 908-924 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 479 | 1 | 7 |
| β-strand | 491-496 | 6 | 8 |
| β-strand | 500-507 | 8 | 8 |
| β-strand | 510-517 | 8 | 8 |
| β-strand | 526-530 | 5 | 8 |
| β-strand | 536-539 | 4 | 9 |
| β-strand | 543-547 | 5 | 9 |
| β-strand | 553-558 | 6 | 9 |
| α-helix | 564-565 | 2 | |
| β-strand | 566-569 | 4 | 9 |
| β-strand | 578-583 | 6 | 7 |
| β-strand | 588-592 | 5 | 7 |
| β-strand | 596-600 | 5 | 7 |
| β-strand | 606-611 | 6 | 7 |
| β-strand | 615-621 | 7 | 10 |
| β-strand | 624-631 | 8 | 10 |
| β-strand | 635-642 | 8 | 10 |
| β-strand | 649-656 | 8 | 10 |
| α-helix | 674-679 | 6 | |
| β-strand | 686-689 | 4 | 1 |
| β-strand | 695-698 | 4 | 1 |
| β-strand | 703-708 | 6 | 1 |
| β-strand | 717-723 | 7 | 1 |
| α-helix | 724-731 | 8 | |
| β-strand | 740-748 | 9 | 11 |
| β-strand | 751-758 | 8 | 11 |
| α-helix | 768 | 1 | |
| β-strand | 772-775 | 4 | 11 |
| β-strand | 777 | 1 | 1 |
| α-helix | 783-789 | 7 | |
| α-helix | 819-844 | 26 | |
| α-helix | 851-874 | 24 | |
| α-helix | 879-886 | 8 | |
| α-helix | 892-904 | 13 | |
| α-helix | 908-922 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 491-496 | 6 | 12 |
| β-strand | 500-507 | 8 | 12 |
| β-strand | 510-517 | 8 | 12 |
| β-strand | 526-530 | 5 | 12 |
| β-strand | 536-539 | 4 | 13 |
| β-strand | 543-547 | 5 | 13 |
| β-strand | 553-558 | 6 | 13 |
| α-helix | 564-565 | 2 | |
| β-strand | 566-569 | 4 | 13 |
| β-strand | 578-583 | 6 | 5 |
| β-strand | 588-592 | 5 | 5 |
| β-strand | 596-600 | 5 | 5 |
| β-strand | 606-611 | 6 | 5 |
| α-helix | 614 | 1 | |
| β-strand | 615-621 | 7 | 14 |
| β-strand | 624-631 | 8 | 14 |
| β-strand | 635-643 | 9 | 14 |
| β-strand | 648-656 | 9 | 14 |
| α-helix | 674-679 | 6 | |
| β-strand | 686-689 | 4 | 7 |
| β-strand | 695-698 | 4 | 7 |
| β-strand | 703-708 | 6 | 7 |
| β-strand | 717-723 | 7 | 7 |
| α-helix | 724-731 | 8 | |
| β-strand | 740-748 | 9 | 15 |
| β-strand | 751-758 | 8 | 15 |
| α-helix | 768 | 1 | |
| β-strand | 772-775 | 4 | 15 |
| β-strand | 777 | 1 | 7 |
| α-helix | 783-792 | 10 | |
| α-helix | 819-844 | 26 | |
| α-helix | 851-874 | 24 | |
| α-helix | 879-886 | 8 | |
| α-helix | 892-904 | 13 | |
| α-helix | 908-923 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CTF4 | A, B, C | protein | 478 | SACCHAROMYCES CEREVISIAE | Q01454 (AlphaFold model) |
>4C8H_1 CTF4 (chains A, B, C) MGSSHHHHHHSQDPENLYFQGTGKFRYMPFSPAGTPFGFTDRRYLTMNEVGYVSTVKNSE QYSITVSFFDVGRFREYHFEDLFGYDLCFLNEKGTLFGQSKTGQIQYRPHDSIHSNWTKI IPLQAGERITSVAATPVRVIVGTSLGYFRSFNQFGVPFAVEKTSPIVALTAQNYRVFSVH YSQFHGLSYSLSELGTSSKRYYKRECPLPMSLPNINSDMKKDANLDYYNFNPMGIKSLFF SSYGDPCIFGSDNTLLLLSKWRSPEESKWLPILDSNMEIWKMSGGKETTDIHVWPLALAY DTLNCILVKGKHIWPEFPLPLPSEMEIRMPVFVKSKLLEENKAILNKKNEIGADTEAEEG EEDKEIQIPVSMAAEEEYLRSKVLSELLTDTLENDGEMYGNENEVLAALNGAYDKALLRL FASACSDQNVEKALSLAHELKQDRALTAAVKISERAELPSLVKKINNIREARYEQQLK
A Ctf4 Trimer Couples the Cmg Helicase to DNA Polymerase Alpha in the Eukaryotic Replisome. Simon, A.C., Zhou, J.C., Perera, R.L. et al. Nature (2014) 510:293. DOI 10.1038/NATURE13234 · PubMed
Other PDB entries of the same protein (UniProt Q01454 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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