Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - Apo closed P-loop conformation. Determined by X-ray diffraction at 1.9 Å resolution. Released 11 Sept 2024.
Explore 8RO8 in 3D Show helices and sheets RCSB PDB PDBe
8RO8 contains 19 α-helices and 19 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 |
|---|---|---|---|
| β-strand | 3-12 | 10 | 1 |
| β-strand | 15-21 | 7 | 1 |
| β-strand | 27-31 | 5 | 2 |
| α-helix | 37-48 | 12 | |
| α-helix | 53-55 | 3 | |
| α-helix | 61-64 | 4 | |
| β-strand | 65 | 1 | 1 |
| α-helix | 68-70 | 3 | |
| β-strand | 77-85 | 9 | 1 |
| β-strand | 92-99 | 8 | 1 |
| β-strand | 102-107 | 6 | 1 |
| β-strand | 110-112 | 3 | 1 |
| α-helix | 114-122 | 9 | |
| β-strand | 134-135 | 2 | 2 |
| α-helix | 139-144 | 6 | |
| α-helix | 148-158 | 11 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-176 | 12 | |
| α-helix | 1055-1089 | 35 | |
| β-strand | 1095-1100 | 6 | 3 |
| α-helix | 1106-1108 | 3 | |
| β-strand | 1111-1116 | 6 | 3 |
| β-strand | 1122-1124 | 3 | 3 |
| α-helix | 1125-1127 | 3 | |
| α-helix | 1130-1145 | 16 | |
| β-strand | 1152-1156 | 5 | 2 |
| α-helix | 1167-1180 | 14 | |
| β-strand | 1183-1187 | 5 | 2 |
| α-helix | 1191-1194 | 4 | |
| β-strand | 1199-1206 | 8 | 2 |
| β-strand | 1212-1219 | 8 | 2 |
| α-helix | 1220-1222 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 579-580 | 2 | 4 |
| α-helix | 581-584 | 4 | |
| α-helix | 590-605 | 16 | |
| β-strand | 609-613 | 5 | 4 |
| β-strand | 620-624 | 5 | 4 |
| α-helix | 632-635 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Structural maintenance of chromosomes protein 1A | A | protein | 456 | Homo sapiens | Q14683 (AlphaFold model) |
| 64-kDa C-terminal product | B | protein | 81 | Homo sapiens | O60216 (AlphaFold model) |
>8RO8_1 Structural maintenance of chromosomes protein 1A (chains A) MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKT LRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEE LEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEE DTQFNYHRKKNIAAERKEAKESSKHPTSLVPRGSDAQAEEEIKQEMNTLQQKLNEQQSVL QRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESV ATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAA LALLFAIHSYKPAPFFVLDQIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKA ESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ
>8RO8_2 64-kDa C-terminal product (chains B) MKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEP YSDIIATPGPRFHGSLEVLFQ
The cohesin ATPase cycle is mediated by specific conformational dynamics and interface plasticity of SMC1A and SMC3 ATPase domains. Vitoria Gomes, M., Landwerlin, P., Diebold-Durand, M.L. et al. Cell Rep (2024) 43:114656-114656. DOI 10.1016/j.celrep.2024.114656 · PubMed
Other PDB entries of the same protein (UniProt Q14683 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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