Structure of the Pds5-Scc1 complex and implications for cohesin function. Determined by X-ray diffraction at 5.8 Å resolution. Released 2 Mar 2016.
Explore 5FRR in 3D Show helices and sheets RCSB PDB PDBe
5FRR contains 91 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 | 25-41 | 17 | |
| α-helix | 50-52 | 3 | |
| α-helix | 53-56 | 4 | |
| α-helix | 62-65 | 4 | |
| α-helix | 70-87 | 18 | |
| α-helix | 95-113 | 19 | |
| α-helix | 120-132 | 13 | |
| α-helix | 137-139 | 3 | |
| α-helix | 145-156 | 12 | |
| α-helix | 168-179 | 12 | |
| α-helix | 187-194 | 8 | |
| α-helix | 196-199 | 4 | |
| α-helix | 215-225 | 11 | |
| α-helix | 228-248 | 21 | |
| α-helix | 255-272 | 18 | |
| α-helix | 277-279 | 3 | |
| α-helix | 281-288 | 8 | |
| α-helix | 293-306 | 14 | |
| α-helix | 315-318 | 4 | |
| α-helix | 320-326 | 7 | |
| α-helix | 327-331 | 5 | |
| α-helix | 335-342 | 8 | |
| α-helix | 345-351 | 7 | |
| α-helix | 358-366 | 9 | |
| α-helix | 372-379 | 8 | |
| α-helix | 381-384 | 4 | |
| α-helix | 387-392 | 6 | |
| α-helix | 397-405 | 9 | |
| α-helix | 406-408 | 3 | |
| α-helix | 412-428 | 17 | |
| α-helix | 440-446 | 7 | |
| α-helix | 449-455 | 7 | |
| α-helix | 462-472 | 11 | |
| α-helix | 484-494 | 11 | |
| α-helix | 499-510 | 12 | |
| α-helix | 512-526 | 15 | |
| α-helix | 527-529 | 3 | |
| α-helix | 540-547 | 8 | |
| α-helix | 561-564 | 4 | |
| α-helix | 567-574 | 8 | |
| α-helix | 577-584 | 8 | |
| α-helix | 593-606 | 14 | |
| α-helix | 627-637 | 11 | |
| α-helix | 648-653 | 6 | |
| α-helix | 662-675 | 14 | |
| α-helix | 683-690 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-39 | 15 | |
| α-helix | 50-52 | 3 | |
| α-helix | 53-56 | 4 | |
| α-helix | 62-65 | 4 | |
| α-helix | 70-86 | 17 | |
| α-helix | 95-113 | 19 | |
| α-helix | 120-132 | 13 | |
| α-helix | 137-139 | 3 | |
| α-helix | 145-156 | 12 | |
| α-helix | 165-167 | 3 | |
| α-helix | 168-179 | 12 | |
| α-helix | 187-194 | 8 | |
| α-helix | 196-199 | 4 | |
| α-helix | 215-225 | 11 | |
| α-helix | 228-247 | 20 | |
| α-helix | 255-272 | 18 | |
| α-helix | 277-288 | 12 | |
| α-helix | 293-306 | 14 | |
| α-helix | 315-318 | 4 | |
| α-helix | 320-327 | 8 | |
| α-helix | 328-331 | 4 | |
| α-helix | 335-342 | 8 | |
| α-helix | 345-351 | 7 | |
| α-helix | 358-366 | 9 | |
| α-helix | 372-379 | 8 | |
| α-helix | 381-384 | 4 | |
| α-helix | 387-393 | 7 | |
| α-helix | 397-405 | 9 | |
| α-helix | 406-408 | 3 | |
| α-helix | 412-428 | 17 | |
| α-helix | 440-446 | 7 | |
| α-helix | 449-454 | 6 | |
| α-helix | 457-459 | 3 | |
| α-helix | 462-471 | 10 | |
| α-helix | 472-476 | 5 | |
| α-helix | 483-494 | 12 | |
| α-helix | 499-526 | 28 | |
| α-helix | 544-554 | 11 | |
| α-helix | 561-572 | 12 | |
| α-helix | 579-585 | 7 | |
| α-helix | 593-608 | 16 | |
| α-helix | 630-640 | 11 | |
| α-helix | 649-653 | 5 | |
| α-helix | 662-678 | 17 | |
| α-helix | 686-695 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sister chromatid cohesion protein PDS5 | A, B | protein | 703 | SACCHAROMYCES CEREVISIAE | Q04264 (AlphaFold model) |
>5FRR_1 SISTER CHROMATID COHESION PROTEIN PDS5 (chains A, B) GAMAKGAVTKLKFNSPIISTSDQLISTNELLDRLKALHEELASLDQDNTDLTGLDKYRDA LVSRKLLKHKDVGIRAFTACCLSDILRLYAPDAPYTDAQLTDIFKLVLSQFEQLGDQENG YHIQQTYLITKLLEYRSIVLLADLPSSNNLLIELFHIFYDPNKSFPARLFNVIGGILGEV ISEFDSVPLEVLRLIFNKFLTYNPNEIPEGLNVTSDCGYEVSLILCDTYSNRMSRHLTKY YSEIIHEATNDDNNSRLLTVVVKLHKLVLRLWETVPELINAVIGFIYHELSSENELFRKE ATKLIGQILTSYSDLNFVSTHSDTFKAWISKIADISPDVRVEWTESIPQIIATREDISKE LNQALAKTFIDSDPRVRRTSVMIFNKVPVTEIWKNITNKAIYTSLLHLAREKHKEVRELC INTMAKFYSNSLNEIERTYQNKEIWEIIDTIPSTLYNLYYINDLNINEQVDSVIFEYLLP FEPDNDKRVHRLLTVLSHFDKKAFTSFFAFNARQIKISFAISKYIDFSKFLNNQESMSSS QGPIVMNKYNQTLQWLASGLSDSTKAIDALETIKQFNDERIFYLLNACVTNDIPFLTFKN CYNELVSKLQTPGLFKKYNISTGASIMPRDIAKVIQILLFRASPIIYNVSNISVLLNLSN NSDAKQLDLKRRILDDISKVNPTLFKDQIRTLKTIIKDLDDPD
Structure of the Pds5-Scc1 Complex and Implications for Cohesin Function. Muir, K.W., Kschonsak, M., Li, Y. et al. Cell Rep (2016) 14:2116. DOI 10.1016/J.CELREP.2016.01.078 · PubMed
Other PDB entries of the same protein (UniProt Q04264 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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