Structure of the Pds5-Scc1 complex and implications for cohesin function. Determined by X-ray diffraction at 2.9 Å resolution. Released 2 Mar 2016.
Explore 5FRP in 3D Show helices and sheets RCSB PDB PDBe
5FRP contains 87 α-helices and 4 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 |
|---|---|---|---|
| α-helix | 25-41 | 17 | |
| α-helix | 53-58 | 6 | |
| α-helix | 62-65 | 4 | |
| α-helix | 70-87 | 18 | |
| α-helix | 95-113 | 19 | |
| α-helix | 120-132 | 13 | |
| α-helix | 136-141 | 6 | |
| α-helix | 145-157 | 13 | |
| α-helix | 165-167 | 3 | |
| α-helix | 168-180 | 13 | |
| α-helix | 187-199 | 13 | |
| α-helix | 215-226 | 12 | |
| α-helix | 228-247 | 20 | |
| α-helix | 254-272 | 19 | |
| α-helix | 274-279 | 6 | |
| α-helix | 281-288 | 8 | |
| α-helix | 293-306 | 14 | |
| α-helix | 315-318 | 4 | |
| α-helix | 320-327 | 8 | |
| α-helix | 328-331 | 4 | |
| α-helix | 335-343 | 9 | |
| α-helix | 345-351 | 7 | |
| α-helix | 358-366 | 9 | |
| α-helix | 372-384 | 13 | |
| α-helix | 387-393 | 7 | |
| α-helix | 397-405 | 9 | |
| α-helix | 406-408 | 3 | |
| β-strand | 409 | 1 | 1 |
| α-helix | 412-431 | 20 | |
| α-helix | 440-446 | 7 | |
| α-helix | 449-455 | 7 | |
| α-helix | 456-459 | 4 | |
| α-helix | 462-471 | 10 | |
| α-helix | 472-476 | 5 | |
| α-helix | 483-495 | 13 | |
| α-helix | 499-526 | 28 | |
| α-helix | 527-529 | 3 | |
| α-helix | 540-555 | 16 | |
| α-helix | 561-574 | 14 | |
| α-helix | 577-587 | 11 | |
| α-helix | 593-607 | 15 | |
| α-helix | 626-640 | 15 | |
| α-helix | 648-653 | 6 | |
| α-helix | 662-678 | 17 | |
| α-helix | 683-690 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-41 | 17 | |
| α-helix | 53-58 | 6 | |
| α-helix | 62-65 | 4 | |
| α-helix | 70-87 | 18 | |
| α-helix | 95-112 | 18 | |
| α-helix | 120-132 | 13 | |
| α-helix | 135-141 | 7 | |
| α-helix | 145-157 | 13 | |
| α-helix | 165-167 | 3 | |
| α-helix | 168-180 | 13 | |
| α-helix | 187-199 | 13 | |
| α-helix | 215-226 | 12 | |
| α-helix | 228-247 | 20 | |
| α-helix | 254-272 | 19 | |
| α-helix | 274-279 | 6 | |
| α-helix | 281-288 | 8 | |
| α-helix | 293-306 | 14 | |
| α-helix | 315-318 | 4 | |
| α-helix | 320-327 | 8 | |
| α-helix | 328-331 | 4 | |
| α-helix | 335-351 | 17 | |
| α-helix | 358-366 | 9 | |
| α-helix | 372-384 | 13 | |
| α-helix | 387-393 | 7 | |
| α-helix | 397-405 | 9 | |
| α-helix | 406-408 | 3 | |
| β-strand | 409 | 1 | 2 |
| α-helix | 412-431 | 20 | |
| α-helix | 440-446 | 7 | |
| α-helix | 449-456 | 8 | |
| α-helix | 457-459 | 3 | |
| α-helix | 462-471 | 10 | |
| α-helix | 472-476 | 5 | |
| α-helix | 483-495 | 13 | |
| α-helix | 499-526 | 28 | |
| α-helix | 544-554 | 11 | |
| α-helix | 555-557 | 3 | |
| α-helix | 561-572 | 12 | |
| α-helix | 579-587 | 9 | |
| α-helix | 593-608 | 16 | |
| α-helix | 630-640 | 11 | |
| α-helix | 648-653 | 6 | |
| α-helix | 662-678 | 17 | |
| α-helix | 684-696 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 127 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sister chromatid cohesion protein PDS5 | A, B | protein | 703 | SACCHAROMYCES CEREVISIAE | Q04264 (AlphaFold model) |
| MCD1-like protein | C, D | protein | 44 | SACCHAROMYCES CEREVISIAE | Q12158 (AlphaFold model) |
>5FRP_1 SISTER CHROMATID COHESION PROTEIN PDS5 (chains A, B) GAMAKGAVTKLKFNSPIISTSDQLISTNELLDRLKALHEELASLDQDNTDLTGLDKYRDA LVSRKLLKHKDVGIRAFTACCLSDILRLYAPDAPYTDAQLTDIFKLVLSQFEQLGDQENG YHIQQTYLITKLLEYRSIVLLADLPSSNNLLIELFHIFYDPNKSFPARLFNVIGGILGEV ISEFDSVPLEVLRLIFNKFLTYNPNEIPEGLNVTSDCGYEVSLILCDTYSNRMSRHLTKY YSEIIHEATNDDNNSRLLTVVVKLHKLVLRLWETVPELINAVIGFIYHELSSENELFRKE ATKLIGQILTSYSDLNFVSTHSDTFKAWISKIADISPDVRVEWTESIPQIIATREDISKE LNQALAKTFIDSDPRVRRTSVMIFNKVPVTEIWKNITNKAIYTSLLHLAREKHKEVRELC INTMAKFYSNSLNEIERTYQNKEIWEIIDTIPSTLYNLYYINDLNINEQVDSVIFEYLLP FEPDNDKRVHRLLTVLSHFDKKAFTSFFAFNARQIKISFAISKYIDFSKFLNNQESMSSS QGPIVMNKYNQTLQWLASGLSDSTKAIDALETIKQFNDERIFYLLNACVTNDIPFLTFKN CYNELVSKLQTPGLFKKYNISTGASIMPRDIAKVIQILLFRASPIIYNVSNISVLLNLSN NSDAKQLDLKRRILDDISKVNPTLFKDQIRTLKTIIKDLDDPD
>5FRP_2 MCD1-LIKE PROTEIN (chains C, D) RLNTVTRVHQLMLEDAVTEREVLVTPGLEFLDDTTIPVGLMAQE
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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