9Q2I: Rad55-Rad57-SHU homologous recombination complex

Rad55-Rad57-SHU homologous recombination complex. Determined by electron microscopy at 3.0 Å resolution. Released 22 Jul 2026.

Method: Electron microscopy
Resolution: 3.0 Å
Organisms: Saccharomyces cerevisiae, synthetic construct
Chains: 9
Atoms: 16,874
Mol. weight: 322.93 kDa
Ligands: ADP, ZN, ATP, MG
Released: 22 Jul 2026

Explore 9Q2I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q2I contains 118 α-helices and 95 β-strands across 8 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: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
α-helix	7-11	5
α-helix	15-17	3
β-strand	18	1	2
α-helix	19	1
α-helix	23-28	6
β-strand	33	1	2
α-helix	34	1
β-strand	37-42	6	3
α-helix	49-66	18
β-strand	74-78	5	3
α-helix	82-83	2
α-helix	85-91	7
α-helix	96-101	6
β-strand	102-106	5	3
α-helix	110-122	13
β-strand	131-135	5	3
α-helix	137-151	15
α-helix	154-158	5
α-helix	161-182	22
β-strand	185-189	5	3
β-strand	193-195	3	4
β-strand	233-235	3	4
α-helix	249-252	4
β-strand	255-260	6	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: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	16-19	4
α-helix	24-27	4
α-helix	32-41	10
α-helix	45-50	6
α-helix	53-60	8
α-helix	64-86	23
β-strand	90	1	3
β-strand	99-100	2	5
α-helix	105-111	7
β-strand	115-116	2	5
β-strand	119-124	6	6
α-helix	131-141	11
β-strand	155-159	5	6
α-helix	166-174	9
α-helix	177-182	6
β-strand	189-193	5	6
α-helix	197-202	6
α-helix	203-207	5
α-helix	208-214	7
β-strand	221-225	5	6
α-helix	228-234	7
α-helix	240-264	25
β-strand	267-272	6	6
β-strand	274-276	3	7
α-helix	278-280	3
β-strand	292	1	4
α-helix	293-301	9
α-helix	305-317	13
α-helix	323-327	5
β-strand	329	1	8
α-helix	331-338	8
β-strand	378	1	8
α-helix	379-382	4
β-strand	384-386	3	7
α-helix	390-393	4
β-strand	398-408	11	6
α-helix	410-413	4
α-helix	426-428	3
β-strand	429-440	12	6
β-strand	443	1	6
β-strand	446-453	8	6
β-strand	456-459	4	6

Chain C: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
β-strand	9-13	5	1
α-helix	17-28	12
β-strand	36-41	6	1
α-helix	48-54	7
α-helix	63-66	4
β-strand	71-73	3	1
α-helix	77-95	19
β-strand	111-117	7	1
α-helix	119-129	11
α-helix	132-151	20
β-strand	158-165	8	1
α-helix	167-170	4
α-helix	171-176	6
α-helix	199-206	8
β-strand	210-211	2	1

Chain D: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	10-11	2	9
α-helix	12-15	4
α-helix	17-19	3
α-helix	27-29	3
α-helix	36-40	5
β-strand	43-48	6	10
α-helix	53-54	2
α-helix	55-61	7
β-strand	69-74	6	10
β-strand	89-92	4	10
α-helix	95-98	4
α-helix	100-112	13
α-helix	114-120	7
β-strand	130-136	7	10
α-helix	144	1
β-strand	145	1	11
α-helix	146	1
β-strand	152	1	11
α-helix	154-156	3
α-helix	157-171	15
β-strand	174-179	6	10
α-helix	182-186	5
α-helix	188-190	3
α-helix	213-216	4
β-strand	221-225	5	10
β-strand	235-236	2	10

Chain E: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	3-11	9
β-strand	24-27	4	9
α-helix	31-36	6
α-helix	37-41	5
α-helix	51-55	5
α-helix	56-60	5
β-strand	61-64	4	9
α-helix	69-81	13
β-strand	90-94	5	9
α-helix	96-99	4
α-helix	105-121	17
β-strand	125-129	5	9
α-helix	131-133	3
α-helix	137-149	13

Chain F: 11 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	8-14	7
α-helix	26-35	10
α-helix	41-49	9
β-strand	53-54	2	12
β-strand	57-58	2	13
α-helix	72-79	8
β-strand	94-95	2	12
α-helix	103-104	2
β-strand	105-106	2	12
β-strand	107-108	2	14
β-strand	113-114	2	14
α-helix	117-128	12
α-helix	136-140	5
β-strand	141	1	15
β-strand	169	1	15
α-helix	177-186	10
α-helix	190-194	5
α-helix	195-199	5
β-strand	203-204	2	12
β-strand	207-208	2	13
α-helix	211-219	9

Chain G: 17 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	82	1	16
α-helix	83-85	3
α-helix	93-101	9
β-strand	106	1	16
α-helix	107-112	6
α-helix	115-120	6
α-helix	126-139	14
β-strand	145-146	2	6
α-helix	147-153	7
β-strand	159-160	2	17
α-helix	165-170	6
β-strand	175-176	2	17
β-strand	180-185	6	18
α-helix	191-201	11
α-helix	206-208	3
β-strand	214-219	6	18
α-helix	226-235	10
α-helix	240-245	6
β-strand	247-251	5	18
α-helix	255-269	15
β-strand	274-279	6	18
α-helix	282-289	8
α-helix	295-317	23
β-strand	320-325	6	18
β-strand	327-329	3	19
β-strand	342-344	3	19
α-helix	347-353	7
β-strand	356-362	7	18
β-strand	367-374	8	18
β-strand	382-388	7	18
β-strand	391-393	3	18
α-helix	394-396	3
α-helix	397-399	3

Chain I: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	82	1	20
α-helix	83-86	4
α-helix	93-102	10
β-strand	106	1	20
α-helix	107-111	5
α-helix	115-119	5
α-helix	126-139	14
β-strand	145-146	2	18
α-helix	147-155	9
β-strand	159-160	2	21
α-helix	165-170	6
β-strand	175-176	2	21
β-strand	180-185	6	22
α-helix	191-201	11
α-helix	206-208	3
β-strand	214-219	6	22
α-helix	226-236	11
α-helix	240-245	6
β-strand	247-251	5	22
α-helix	255-271	17
β-strand	274-280	7	22
α-helix	284-289	6
α-helix	293-295	3
α-helix	296-317	22
β-strand	320-325	6	22
β-strand	327-328	2	23
β-strand	343-344	2	23
α-helix	347-353	7
β-strand	356-362	7	22
β-strand	367-374	8	22
β-strand	382-388	7	22
β-strand	391-393	3	22

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
DNA repair protein RAD51	G, I	protein	418	Saccharomyces cerevisiae	P25454
ssDNA (12-mer)	H	DNA	12	synthetic construct

Sequence of entity 1 (A), FASTA

>9Q2I_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

>9Q2I_2 DNA repair protein RAD57 (chains B)
MPRALSIKFDNTYMDLYDELPESKLLYDEEFSYLLDAVRQNGVCVVDFLTLTPKELARLI
QRSINEVFRFQQLLVHEYNEKYLEICEKNSISPDNGPECFTTADVAMDELLGGGIFTHGI
TEIFGESSTGKSQLLMQLALSVQLSEPAGGLGGKCVYITTQGDLPTQRLESMLSSRPAYE
KLGITQSNIFTVSCNDLINQEHIINVQLPILLERSKGSIKLVIIDSISHHLRVELQNKSF
RESQENKNYLDRMAEKLQILAHDYSLSVVVANQVGDKPLANSPVAHRTYVTDYDYQLGWL
VGWKNSTILYRQMNSLLGASSNNDEILSDDEDYMLIERVMSTVNDRNYDFFSKKKPPIIE
NKTVERNSSSPISRQSKKRKFDYRVPNLGLTWSNHVSTRILLQKSFKASTIIQRGEAHLY
KGGDSASFWQVKRTMKVVYSTFAKPGQIAYQITKRGIETA

Sequence of entity 3 (C), FASTA

>9Q2I_3 Chromosome segregation in meiosis protein 2 (chains C)
MEYEDLELITIWPSPTKNKLCQFIKQNLSKEHVVTQLFFIDATSSFPLSQFQKLVPPTLP
ENVRIYENIRINTCLDLEELSAITVKLLQILSMNKINAQRGTEDAVTEPLKIILYINGLE
VMFRNSQFKSSPQRSHELLRDTLLKLRVMGNDENENASIRTLLEFPKEQLLDYYLKKNNN
TRTSSVRSKRRRIKNGDSLAEYIWKYYADSLFE

Sequence of entity 4 (D), FASTA

>9Q2I_4 Platinum sensitivity protein 3 (chains D)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGENLYFQMEVLKNIRIYPLSNFITSTKN
YINLPNELRNLISEEQESKLGFLHIIESDFKPSVALQKLVNCTTGDEKILIIDIVSIWSQ
QKQRQHGAIYMNSLSCINITGLIVFLELLYDSPMDALRRCQVDNFNFQLRGIVIDNLSFL
NFESDKNYDVINLSKFEKLFKILRKLREFLGCWIITKSFPTDFYNGIENTLVDKWSIKRK
SGVTLYPTKLPDSYMKGMDLIIYREVVDGRPQYRRIAALEE

Sequence of entity 5 (E), FASTA

>9Q2I_5 Suppressor of HU sensitivity involved in recombination protein 1 (chains E)
MQFEERLQQLVESDWSLDQSSPNVLVIVLGDTARKYVELGGLKEHVTTNTVAGHVASRER
VSVVFLGRVKYLYMYLTRMQAQANGPQYSNVLVYGLWDLTATQDGPQQLRLLSLVLRQCL
SLPSKVEFYPEPPSSSVPARLLRFWDHIIR

Sequence of entity 6 (F), FASTA

>9Q2I_6 Suppressor of hydroxyurea sensitivity protein 2 (chains F)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGENLYFQGSKDVIEYSKLFAKLVNTNDD
TKLDDTIASFLYYMFPRELFIRAISLLESSDMFIYILDRVHNKEGNEHTSLIDVLVDEFY
KGSSNSLLEYRLIVKDTNDGAPPILVDIAHWFCSCEEFCKYFHEALEKTDEKEELHDVLI
NEVDDHLQFSDDRFAQLDPHSLSKQWYFKFDKVCCSHLLAFSILLRSSINVLKFFTVNSN
KVFVIAIDNIDEWLNLHINIVE

Sequence of entity 7 (G, I), FASTA

>9Q2I_7 DNA repair protein RAD51 (chains G, I)
MHHHHHHHHGENLYFQGSMSQVQEQHISESQLQYGNGSLMSTVPADLSQSVVDGNGNGSS
EDIEATNGSGDGGGLQEQAEAQGEMEDEAYDEAALGSFVPIEKLQVNGITMADVKKLRES
GLHTAEAVAYAPRKDLLEIKGISEAKADKLLNEAARLVPMGFVTAADFHMRRSELICLTT
GSKNLDTLLGGGVETGSITELFGEFRTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEG
TFRPVRLVSIAQRFGLDPDDALNNVAYARAYNADHQLRLLDAAAQMMSESRFSLIVVDSV
MALYRTDFSGRGELSARQMHLAKFMRALQRLADQFGVAVVVTNQVVAQVDGGMAFNPDPK
KPIGGNIMAHSSTTRLGFKKGKGCQRLCKVVDSPCLPEAECVFAIYEDGVGDPREEDE

Sequence of entity 8 (H), FASTA

>9Q2I_8 ssDNA (12-mer) (chains H)
TTTTTTTTTTTT

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
ZN	Zinc ion	Zn	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
MG	Magnesium ion	Mg	4

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
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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