9Q2H: Rad55-Rad57-SHU homologous recombination complex
Rad55-Rad57-SHU homologous recombination complex. Determined by electron microscopy at 2.74 Å resolution. Released 29 Jul 2026.
- Method
- Electron microscopy
- Resolution
- 2.74 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 6
- Atoms
- 11,357
- Mol. weight
- 227.76 kDa
- Ligands
- ADP, MG, ZN
- Released
- 29 Jul 2026
Explore 9Q2H in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9Q2H contains 77 α-helices and 57 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 | 23-28 | 6 | |
| β-strand | 33 | 1 | 2 |
| β-strand | 37-43 | 7 | 3 |
| α-helix | 49-64 | 16 | |
| β-strand | 73-78 | 6 | 3 |
| α-helix | 82-83 | 2 | |
| α-helix | 85-91 | 7 | |
| α-helix | 95-99 | 5 | |
| β-strand | 102-106 | 5 | 3 |
| α-helix | 110-122 | 13 | |
| β-strand | 129-135 | 7 | 3 |
| α-helix | 137-151 | 15 | |
| α-helix | 154-157 | 4 | |
| α-helix | 160-182 | 23 | |
| β-strand | 185-191 | 7 | 3 |
| β-strand | 192-194 | 3 | 4 |
| β-strand | 233 | 1 | 5 |
| β-strand | 234-236 | 3 | 4 |
| α-helix | 249-252 | 4 | |
| β-strand | 255-266 | 12 | 3 |
| β-strand | 305-313 | 9 | 3 |
| β-strand | 338-344 | 7 | 3 |
| β-strand | 351-353 | 3 | 3 |
Chain B: 20 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 16-19 | 4 | |
| α-helix | 24-26 | 3 | |
| α-helix | 29-41 | 13 | |
| α-helix | 45-48 | 4 | |
| α-helix | 53-60 | 8 | |
| α-helix | 64-87 | 24 | |
| β-strand | 90 | 1 | 3 |
| α-helix | 97-98 | 2 | |
| β-strand | 99-100 | 2 | 6 |
| α-helix | 105-108 | 4 | |
| β-strand | 115-116 | 2 | 6 |
| β-strand | 120-125 | 6 | 7 |
| α-helix | 131-141 | 11 | |
| β-strand | 154-159 | 6 | 7 |
| α-helix | 166-174 | 9 | |
| α-helix | 177-181 | 5 | |
| α-helix | 186-188 | 3 | |
| β-strand | 189-193 | 5 | 7 |
| α-helix | 197-202 | 6 | |
| α-helix | 203-207 | 5 | |
| α-helix | 208-215 | 8 | |
| β-strand | 219-224 | 6 | 7 |
| α-helix | 229-234 | 6 | |
| α-helix | 244-263 | 20 | |
| β-strand | 267-273 | 7 | 7 |
| β-strand | 274-276 | 3 | 8 |
| β-strand | 292 | 1 | 5 |
| α-helix | 293-301 | 9 | |
| α-helix | 305-316 | 12 | |
| β-strand | 384-386 | 3 | 8 |
| α-helix | 389-393 | 5 | |
| β-strand | 396-406 | 11 | 7 |
| β-strand | 431-440 | 10 | 7 |
| β-strand | 446-453 | 8 | 7 |
| β-strand | 456-459 | 4 | 7 |
Chain C: 11 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-5 | 3 | |
| β-strand | 9-13 | 5 | 1 |
| α-helix | 17-27 | 11 | |
| β-strand | 34-41 | 8 | 1 |
| α-helix | 48-54 | 7 | |
| α-helix | 62-68 | 7 | |
| β-strand | 69-73 | 5 | 1 |
| α-helix | 77-96 | 20 | |
| 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 | 171-176 | 6 | |
| α-helix | 199-206 | 8 | |
| β-strand | 210-211 | 2 | 1 |
Chain D: 14 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-5 | 4 | |
| β-strand | 9-10 | 2 | 9 |
| α-helix | 12-14 | 3 | |
| β-strand | 18 | 1 | 10 |
| α-helix | 27-29 | 3 | |
| α-helix | 37-40 | 4 | |
| β-strand | 43-47 | 5 | 11 |
| α-helix | 53-54 | 2 | |
| α-helix | 55-60 | 6 | |
| β-strand | 69-73 | 5 | 11 |
| β-strand | 89-92 | 4 | 11 |
| α-helix | 100-112 | 13 | |
| α-helix | 114-117 | 4 | |
| α-helix | 119-121 | 3 | |
| β-strand | 130-135 | 6 | 11 |
| α-helix | 138-140 | 3 | |
| α-helix | 157-170 | 14 | |
| β-strand | 174-179 | 6 | 11 |
| α-helix | 182-185 | 4 | |
| α-helix | 188-190 | 3 | |
| α-helix | 213-218 | 6 | |
| β-strand | 221-226 | 6 | 11 |
| β-strand | 233-237 | 5 | 11 |
Chain E: 9 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-11 | 9 | |
| α-helix | 13-15 | 3 | |
| β-strand | 24-29 | 6 | 9 |
| α-helix | 30-34 | 5 | |
| β-strand | 48 | 1 | 10 |
| α-helix | 51-59 | 9 | |
| β-strand | 61-66 | 6 | 9 |
| α-helix | 69-81 | 13 | |
| β-strand | 90-94 | 5 | 9 |
| α-helix | 96-100 | 5 | |
| α-helix | 105-119 | 15 | |
| β-strand | 126-129 | 4 | 9 |
| α-helix | 131-133 | 3 | |
| α-helix | 137-148 | 12 | |
Chain F: 11 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-15 | 8 | |
| α-helix | 26-35 | 10 | |
| α-helix | 42-49 | 8 | |
| β-strand | 53-58 | 6 | 12 |
| α-helix | 72-76 | 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 | 136-139 | 4 | |
| β-strand | 141 | 1 | 13 |
| β-strand | 169 | 1 | 13 |
| α-helix | 177-186 | 10 | |
| α-helix | 190-192 | 3 | |
| α-helix | 193-197 | 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 |
Sequence of entity 1 (A), FASTA
>9Q2H_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
>9Q2H_2 DNA repair protein RAD57 (chains B)
MPRALSIKFDNTYMDLYDELPESKLLYDEEFSYLLDAVRQNGVCVVDFLTLTPKELARLI
QRSINEVFRFQQLLVHEYNEKYLEICEKNSISPDNGPECFTTADVAMDELLGGGIFTHGI
TEIFGESSTGKSQLLMQLALSVQLSEPAGGLGGKCVYITTEGDLPTQRLESMLSSRPAYE
KLGITQSNIFTVSCNDLINQEHIINVQLPILLERSKGSIKLVIIDSISHHLRVELQNKSF
RESQENKNYLDRMAEKLQILAHDYSLSVVVANQVGDKPLANSPVAHRTYVTDYDYQLGWL
VGWKNSTILYRQMNSLLGASSNNDEILSDDEDYMLIERVMSTVNDRNYDFFSKKKPPIIE
NKTVERNSSSPISRQSKKRKFDYRVPNLGLTWSNHVSTRILLQKSFKASTIIQRGEAHLY
KGGDSASFWQVKRTMKVVYSTFAKPGQIAYQITKRGIETA
Sequence of entity 3 (C), FASTA
>9Q2H_3 Chromosome segregation in meiosis protein 2 (chains C)
MEYEDLELITIWPSPTKNKLCQFIKQNLSKEHVVTQLFFIDATSSFPLSQFQKLVPPTLP
ENVRIYENIRINTCLDLEELSAITVKLLQILSMNKINAQRGTEDAVTEPLKIILYINGLE
VMFRNSQFKSSPQRSHELLRDTLLKLRVMGNDENENASIRTLLEFPKEQLLDYYLKKNNN
TRTSSVRSKRRRIKNGDSLAEYIWKYYADSLFE
Sequence of entity 4 (D), FASTA
>9Q2H_4 Platinum sensitivity protein 3 (chains D)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGENLYFQMEVLKNIRIYPLSNFITSTKN
YINLPNELRNLISEEQESKLGFLHIIESDFKPSVALQKLVNCTTGDEKILIIDIVSIWSQ
QKQRQHGAIYMNSLSCINITGLIVFLELLYDSPMDALRRCQVDNFNFQLRGIVIDNLSFL
NFESDKNYDVINLSKFEKLFKILRKLREFLGCWIITKSFPTDFYNGIENTLVDKWSIKRK
SGVTLYPTKLPDSYMKGMDLIIYREVVDGRPQYRRIAALEE
Sequence of entity 5 (E), FASTA
>9Q2H_5 Suppressor of HU sensitivity involved in recombination protein 1 (chains E)
MQFEERLQQLVESDWSLDQSSPNVLVIVLGDTARKYVELGGLKEHVTTNTVAGHVASRER
VSVVFLGRVKYLYMYLTRMQAQANGPQYSNVLVYGLWDLTATQDGPQQLRLLSLVLRQCL
SLPSKVEFYPEPPSSSVPARLLRFWDHIIR
Sequence of entity 6 (F), FASTA
>9Q2H_6 Suppressor of hydroxyurea sensitivity protein 2 (chains F)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGENLYFQGSKDVIEYSKLFAKLVNTNDD
TKLDDTIASFLYYMFPRELFIRAISLLESSDMFIYILDRVHNKEGNEHTSLIDVLVDEFY
KGSSNSLLEYRLIVKDTNDGAPPILVDIAHWFCSCEEFCKYFHEALEKTDEKEELHDVLI
NEVDDHLQFSDDRFAQLDPHSLSKQWYFKFDKVCCSHLLAFSILLRSSINVLKFFTVNSN
KVFVIAIDNIDEWLNLHINIVE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| MG | Magnesium ion | Mg | 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
- 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
- 9Q2E 3.44 Å, Rad55-Rad57-SHU bound to ssDNA
- 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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