9Q2E: Rad55-Rad57-SHU
Rad55-Rad57-SHU bound to ssDNA. Determined by electron microscopy at 3.44 Å resolution. Released 22 Jul 2026.
- Method
- Electron microscopy
- Resolution
- 3.44 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 7
- Atoms
- 11,538
- Mol. weight
- 229.54 kDa
- Ligands
- MG, ADP, ZN
- Released
- 22 Jul 2026
Explore 9Q2E in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9Q2E contains 80 α-helices and 61 β-strands across 6 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.
Chain A: 12 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-6 | 2 | 1 |
| α-helix | 7-13 | 7 | |
| α-helix | 15-17 | 3 | |
| β-strand | 18 | 1 | 2 |
| α-helix | 19 | 1 | |
| α-helix | 23-26 | 4 | |
| β-strand | 33 | 1 | 2 |
| β-strand | 38-43 | 6 | 3 |
| α-helix | 49-65 | 17 | |
| β-strand | 74-78 | 5 | 3 |
| α-helix | 85-91 | 7 | |
| α-helix | 96-101 | 6 | |
| β-strand | 102-106 | 5 | 3 |
| α-helix | 110-121 | 12 | |
| β-strand | 131-135 | 5 | 3 |
| α-helix | 137-152 | 16 | |
| α-helix | 154-157 | 4 | |
| α-helix | 160-182 | 23 | |
| β-strand | 185-191 | 7 | 3 |
| β-strand | 192-195 | 4 | 4 |
| β-strand | 233-236 | 4 | 4 |
| α-helix | 249-252 | 4 | |
| β-strand | 258-260 | 3 | 3 |
| β-strand | 263-265 | 3 | 3 |
| β-strand | 306-313 | 8 | 3 |
| β-strand | 338-344 | 7 | 3 |
| β-strand | 351-353 | 3 | 3 |
Chain B: 21 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 16-19 | 4 | |
| α-helix | 24-26 | 3 | |
| α-helix | 32-41 | 10 | |
| α-helix | 45-48 | 4 | |
| α-helix | 53-59 | 7 | |
| α-helix | 64-87 | 24 | |
| β-strand | 90 | 1 | 3 |
| β-strand | 99-100 | 2 | 5 |
| α-helix | 105-110 | 6 | |
| β-strand | 115-116 | 2 | 5 |
| β-strand | 120-124 | 5 | 6 |
| α-helix | 131-141 | 11 | |
| α-helix | 146-148 | 3 | |
| β-strand | 154-159 | 6 | 6 |
| α-helix | 166-175 | 10 | |
| α-helix | 177-180 | 4 | |
| α-helix | 186-188 | 3 | |
| β-strand | 189-193 | 5 | 6 |
| α-helix | 197-202 | 6 | |
| α-helix | 203-207 | 5 | |
| α-helix | 208-215 | 8 | |
| β-strand | 219-224 | 6 | 6 |
| α-helix | 229-234 | 6 | |
| α-helix | 240-263 | 24 | |
| β-strand | 267-272 | 6 | 6 |
| β-strand | 274-276 | 3 | 7 |
| β-strand | 292 | 1 | 4 |
| α-helix | 293-296 | 4 | |
| α-helix | 297-299 | 3 | |
| α-helix | 305-316 | 12 | |
| β-strand | 384-386 | 3 | 7 |
| α-helix | 389-393 | 5 | |
| β-strand | 396-406 | 11 | 6 |
| β-strand | 431-440 | 10 | 6 |
| β-strand | 446-453 | 8 | 6 |
| β-strand | 456-459 | 4 | 6 |
Chain C: 11 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-5 | 3 | |
| β-strand | 9-13 | 5 | 1 |
| α-helix | 17-26 | 10 | |
| β-strand | 34-41 | 8 | 1 |
| α-helix | 48-54 | 7 | |
| α-helix | 63-66 | 4 | |
| β-strand | 69-73 | 5 | 1 |
| α-helix | 77-95 | 19 | |
| α-helix | 108-109 | 2 | |
| β-strand | 110-117 | 8 | 1 |
| α-helix | 119-129 | 11 | |
| α-helix | 132-149 | 18 | |
| β-strand | 157-165 | 9 | 1 |
| α-helix | 167-170 | 4 | |
| α-helix | 171-177 | 7 | |
| α-helix | 199-206 | 8 | |
| β-strand | 210-211 | 2 | 1 |
Chain D: 15 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-5 | 4 | |
| α-helix | 7-9 | 3 | |
| β-strand | 10-11 | 2 | 8 |
| α-helix | 12-14 | 3 | |
| α-helix | 18-21 | 4 | |
| α-helix | 36-40 | 5 | |
| β-strand | 43-47 | 5 | 9 |
| α-helix | 53-54 | 2 | |
| α-helix | 55-59 | 5 | |
| β-strand | 65 | 1 | 9 |
| β-strand | 68-73 | 6 | 9 |
| β-strand | 89-91 | 3 | 9 |
| α-helix | 95-97 | 3 | |
| α-helix | 100-112 | 13 | |
| α-helix | 114-120 | 7 | |
| β-strand | 129-135 | 7 | 9 |
| α-helix | 138-140 | 3 | |
| β-strand | 152 | 1 | 10 |
| α-helix | 155-170 | 16 | |
| β-strand | 174-179 | 6 | 9 |
| α-helix | 182-186 | 5 | |
| α-helix | 188-190 | 3 | |
| β-strand | 196 | 1 | 10 |
| α-helix | 213-217 | 5 | |
| β-strand | 221-226 | 6 | 9 |
| β-strand | 233-236 | 4 | 9 |
Chain E: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-11 | 9 | |
| β-strand | 24-29 | 6 | 8 |
| α-helix | 30-37 | 8 | |
| α-helix | 51-59 | 9 | |
| β-strand | 61-66 | 6 | 8 |
| α-helix | 69-81 | 13 | |
| β-strand | 90-94 | 5 | 8 |
| α-helix | 96-99 | 4 | |
| α-helix | 105-120 | 16 | |
| β-strand | 125-129 | 5 | 8 |
| α-helix | 131-133 | 3 | |
| α-helix | 137-149 | 13 | |
Chain F: 13 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-14 | 7 | |
| β-strand | 16 | 1 | 11 |
| β-strand | 24 | 1 | 11 |
| α-helix | 28-30 | 3 | |
| α-helix | 32-34 | 3 | |
| α-helix | 40-50 | 11 | |
| β-strand | 53-58 | 6 | 12 |
| α-helix | 72-75 | 4 | |
| α-helix | 76-80 | 5 | |
| β-strand | 91-95 | 5 | 12 |
| α-helix | 103-104 | 2 | |
| β-strand | 105-108 | 4 | 12 |
| β-strand | 113-114 | 2 | 12 |
| α-helix | 117-128 | 12 | |
| α-helix | 136-140 | 5 | |
| β-strand | 141-144 | 4 | 13 |
| β-strand | 157-158 | 2 | 13 |
| β-strand | 166-169 | 4 | 13 |
| α-helix | 177-186 | 10 | |
| α-helix | 191-194 | 4 | |
| α-helix | 195-199 | 5 | |
| β-strand | 204-208 | 5 | 12 |
| α-helix | 211-218 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Methylated-DNA--protein-cysteine methyltransferase,DNA repair protein RAD55 | A | protein | 631 | Saccharomyces cerevisiae | E5BBQ0 (AlphaFold model), P38953 (AlphaFold model) |
| DNA repair protein RAD57 | B | protein | 460 | Saccharomyces cerevisiae | P25301 (AlphaFold model) |
| Chromosome segregation in meiosis protein 2 | C | protein | 213 | Saccharomyces cerevisiae | P40465 (AlphaFold model) |
| Platinum sensitivity protein 3 | D | protein | 281 | Saccharomyces cerevisiae | Q12318 |
| Suppressor of HU sensitivity involved in recombination protein 1 | E | protein | 150 | Saccharomyces cerevisiae | P38751 |
| Suppressor of hydroxyurea sensitivity protein 2 | F | protein | 262 | Saccharomyces cerevisiae | C7GVQ9 |
| ssDNA (6-mer) | H | DNA | 6 | Saccharomyces cerevisiae | |
Sequence of entity 1 (A), FASTA
>9Q2E_1 Methylated-DNA--protein-cysteine methyltransferase,DNA repair protein RAD55 (chains A)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKGSMDKDCEMKRTTLDSPLGKLELSGCEQG
LHRIIFLGKGTSAADAVEVPAPAAVLGGPEPLMQATAWLNAYFHQPEAIEEFPVPALHHP
VFQQESFTRQVLWKLLKVVKFGEVISYSHLAALAGNPAATAAVKTALSGNPVPILIPCHR
VVQGDLDVGGYEGGLAVKEWLLAHEGHRLGKPGLGGSENLYFQGSMSLGIPLSQLIVESP
KPLSSGITGLDEILNLGFQARSIYEIFGPPGIGKTNFGIQLVCNSLEGIQQSEINDDKIL
WIETFQEMPINILRERFQKFKIVEENVKRVRITKFGQLLYFFQNLFKLSQSVRYKLVIID
GFSQLVCDHLCTLSKRGGGMIDKTIHELKCRHLILIFTVMTKYTHSTGSTIIVLNDCMNT
AFQSNEFESLEEYYEILDDGSNFFVNSNNERRKNNVHILKSALVANIAMGSKDSTWEVFL
RDRIGLFRDWNEQVDETVFVKSKRVKASSSQSNEGCTTIKEMRINKRNFENLRIAIVFNL
HGEDRKREGRNLKRSRSSDDRNYIVKFDFDKATGQLRDIIDLKPDTANIASFPTLSTSSS
SCSQVFNNIDSNDNPLPNAEGKEEIIYDSEG
Sequence of entity 2 (B), FASTA
>9Q2E_2 DNA repair protein RAD57 (chains B)
MPRALSIKFDNTYMDLYDELPESKLLYDEEFSYLLDAVRQNGVCVVDFLTLTPKELARLI
QRSINEVFRFQQLLVHEYNEKYLEICEKNSISPDNGPECFTTADVAMDELLGGGIFTHGI
TEIFGESSTGKSQLLMQLALSVQLSEPAGGLGGKCVYITTEGDLPTQRLESMLSSRPAYE
KLGITQSNIFTVSCNDLINQEHIINVQLPILLERSKGSIKLVIIDSISHHLRVELQNKSF
RESQENKNYLDRMAEKLQILAHDYSLSVVVANQVGDKPLANSPVAHRTYVTDYDYQLGWL
VGWKNSTILYRQMNSLLGASSNNDEILSDDEDYMLIERVMSTVNDRNYDFFSKKKPPIIE
NKTVERNSSSPISRQSKKRKFDYRVPNLGLTWSNHVSTRILLQKSFKASTIIQRGEAHLY
KGGDSASFWQVKRTMKVVYSTFAKPGQIAYQITKRGIETA
Sequence of entity 3 (C), FASTA
>9Q2E_3 Chromosome segregation in meiosis protein 2 (chains C)
MEYEDLELITIWPSPTKNKLCQFIKQNLSKEHVVTQLFFIDATSSFPLSQFQKLVPPTLP
ENVRIYENIRINTCLDLEELSAITVKLLQILSMNKINAQRGTEDAVTEPLKIILYINGLE
VMFRNSQFKSSPQRSHELLRDTLLKLRVMGNDENENASIRTLLEFPKEQLLDYYLKKNNN
TRTSSVRSKRRRIKNGDSLAEYIWKYYADSLFE
Sequence of entity 4 (D), FASTA
>9Q2E_4 Platinum sensitivity protein 3 (chains D)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGENLYFQMEVLKNIRIYPLSNFITSTKN
YINLPNELRNLISEEQESKLGFLHIIESDFKPSVALQKLVNCTTGDEKILIIDIVSIWSQ
QKQRQHGAIYMNSLSCINITGLIVFLELLYDSPMDALRRCQVDNFNFQLRGIVIDNLSFL
NFESDKNYDVINLSKFEKLFKILRKLREFLGCWIITKSFPTDFYNGIENTLVDKWSIKRK
SGVTLYPTKLPDSYMKGMDLIIYREVVDGRPQYRRIAALEE
Sequence of entity 5 (E), FASTA
>9Q2E_5 Suppressor of HU sensitivity involved in recombination protein 1 (chains E)
MQFEERLQQLVESDWSLDQSSPNVLVIVLGDTARKYVELGGLKEHVTTNTVAGHVASRER
VSVVFLGRVKYLYMYLTRMQAQANGPQYSNVLVYGLWDLTATQDGPQQLRLLSLVLRQCL
SLPSKVEFYPEPPSSSVPARLLRFWDHIIR
Sequence of entity 6 (F), FASTA
>9Q2E_6 Suppressor of hydroxyurea sensitivity protein 2 (chains F)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGENLYFQGSKDVIEYSKLFAKLVNTNDD
TKLDDTIASFLYYMFPRELFIRAISLLESSDMFIYILDRVHNKEGNEHTSLIDVLVDEFY
KGSSNSLLEYRLIVKDTNDGAPPILVDIAHWFCSCEEFCKYFHEALEKTDEKEELHDVLI
NEVDDHLQFSDDRFAQLDPHSLSKQWYFKFDKVCCSHLLAFSILLRSSINVLKFFTVNSN
KVFVIAIDNIDEWLNLHINIVE
Sequence of entity 7 (H), FASTA
>9Q2E_7 ssDNA (6-mer) (chains H)
TTTTTT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| ZN | Zinc ion | Zn | 1 |
Primary citation
Yeast Rad55-Rad57-SHU paralog complex dynamically promotes Rad51 filament formation. Koo, C.W., Gore, S.K., Ro, S.Y. et al. Mol Cell (2026) 86:3639. DOI 10.1016/j.molcel.2026.06.045 · PubMed
Other PDB entries of the same protein (UniProt E5BBQ0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3KZY 1.9 Å, Crystal structure of SNAP-tag
- 6Y8P 2.3 Å, Crystal structure of SNAP-tag labeled with a benzyl-tetramethylrhodamine fluorophore
- 8TK7 2.53 Å, Myxococcus xanthus EncA protein shell with compartmentalized SNAP-tag cargo protein
- 9Q2H 2.74 Å, Rad55-Rad57-SHU homologous recombination complex
- 9Q2I 3.0 Å, Rad55-Rad57-SHU homologous recombination complex
- 9Q2C 3.06 Å, Rad55-Rad57-SHU-Rad51 bound to ssDNA with AMP-PNP
- 9Q2F 3.06 Å, Rad55-Rad57-SHU-Rad51-Rad51 bound to ssDNA with AMP-PNP
- 8DD7 3.3 Å, The Cryo-EM structure of Drosophila Cryptochrome in complex with Timeless
- 9Q2L 3.7 Å, Rad55-Rad57(E161Q)-SHU-3xRad51 bound to ssDNA with ATP
- 6RLA 3.9 Å, Structure of the dynein-2 complex; motor domains
- 6SC2 3.9 Å, Structure of the dynein-2 complex; IFT-train bound model
- 6RLB 4.5 Å, Structure of the dynein-2 complex; tail domain
Browse structure collections
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