Cohesin subunit Scc3 from yeast, 674-1072. Determined by X-ray diffraction at 2.1 Å resolution. Released 20 Aug 2014.
Explore 4UVJ in 3D Show helices and sheets RCSB PDB PDBe
4UVJ contains 56 α-helices and 0 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 | 675 | 1 | |
| α-helix | 676-680 | 5 | |
| α-helix | 681-691 | 11 | |
| α-helix | 700-707 | 8 | |
| α-helix | 721-736 | 16 | |
| α-helix | 746-761 | 16 | |
| α-helix | 764-788 | 25 | |
| α-helix | 798-804 | 7 | |
| α-helix | 805-810 | 6 | |
| α-helix | 811-819 | 9 | |
| α-helix | 826-831 | 6 | |
| α-helix | 832-836 | 5 | |
| α-helix | 837-839 | 3 | |
| α-helix | 840-843 | 4 | |
| α-helix | 844-846 | 3 | |
| α-helix | 849-854 | 6 | |
| α-helix | 858-876 | 19 | |
| α-helix | 894-911 | 18 | |
| α-helix | 914-915 | 2 | |
| α-helix | 920-946 | 27 | |
| α-helix | 953-962 | 10 | |
| α-helix | 969-989 | 21 | |
| α-helix | 993-995 | 3 | |
| α-helix | 1002-1005 | 4 | |
| α-helix | 1007-1009 | 3 | |
| α-helix | 1016-1032 | 17 | |
| α-helix | 1038-1045 | 8 | |
| α-helix | 1053-1058 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 675 | 1 | |
| α-helix | 676-680 | 5 | |
| α-helix | 681-690 | 10 | |
| α-helix | 700-708 | 9 | |
| α-helix | 721-736 | 16 | |
| α-helix | 746-761 | 16 | |
| α-helix | 764-787 | 24 | |
| α-helix | 798-804 | 7 | |
| α-helix | 805-810 | 6 | |
| α-helix | 811-819 | 9 | |
| α-helix | 826-831 | 6 | |
| α-helix | 832-836 | 5 | |
| α-helix | 837-839 | 3 | |
| α-helix | 840-843 | 4 | |
| α-helix | 844-846 | 3 | |
| α-helix | 849-854 | 6 | |
| α-helix | 858-877 | 20 | |
| α-helix | 894-911 | 18 | |
| α-helix | 914-915 | 2 | |
| α-helix | 920-946 | 27 | |
| α-helix | 953-962 | 10 | |
| α-helix | 969-990 | 22 | |
| α-helix | 992-995 | 4 | |
| α-helix | 1002-1006 | 5 | |
| α-helix | 1007-1009 | 3 | |
| α-helix | 1016-1032 | 17 | |
| α-helix | 1038-1045 | 8 | |
| α-helix | 1053-1058 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cohesin subunit SCC3 | A, B | protein | 406 | SACCHAROMYCES CEREVISIAE | P40541 (AlphaFold model) |
>4UVJ_1 COHESIN SUBUNIT SCC3 (chains A, B) MDSVKEIVLPLFYDLLNAASIESADILCPLLESFITFSLDDWISIGYETELKKITDKTIK AFMDSTIGNSKVDMKYDIFAKFIHHIHHFEKKELQEKFLNQIATLKIHLKKFLQEKMDPN NSRDDYKDLTCSLYELYINKLTILGRDYPIEVDEELLQLFLNNFVSRIPIMFQDFDDSTA QEINFKMLVLLATWNLEKWREIIEKVRDYENSISKDLRSVWKPIAAIIGRLNTLVISLAA TNETFENINSLFYLKWSACTSLMDIIVAIKIFELKLPADATTWRYSMSEQFPFYLHDNAS KVLLKIFLYLESLFAKQVDVQLERVADEDANLNDLPETGFFENIETEFLLFTVKLKGLMK LNILDERFASRVALNKEKLGPLFKKIVDDTIMENPEPNKKHHHHHH
Structure and Function of Cohesins Scc3/Sa Regulatory Subunit. Roig, M.B., Lowe, J., Chan, K.L. et al. FEBS Lett (2014) 588:3692. DOI 10.1016/J.FEBSLET.2014.08.015 · PubMed
Other PDB entries of the same protein (UniProt P40541 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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