9Q2C: Rad55-Rad57-SHU-Rad51

Rad55-Rad57-SHU-Rad51 bound to ssDNA with AMP-PNP. Determined by electron microscopy at 3.06 Å resolution. Released 22 Jul 2026.

Method: Electron microscopy
Resolution: 3.06 Å
Organisms: Saccharomyces cerevisiae AWRI1631, Saccharomyces cerevisiae, synthetic construct
Chains: 8
Atoms: 14,316
Mol. weight: 276.22 kDa
Ligands: ANP, ZN, MG, ADP
Released: 22 Jul 2026

Explore 9Q2C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q2C contains 94 α-helices and 79 β-strands across 7 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: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	6
α-helix	7-11	5
α-helix	15-17	3
β-strand	18	1	7
α-helix	19	1
α-helix	23-28	6
β-strand	33	1	7
β-strand	37-42	6	8
α-helix	49-66	18
β-strand	74-78	5	8
α-helix	82-83	2
α-helix	85-91	7
α-helix	96-101	6
β-strand	102-106	5	8
α-helix	110-122	13
β-strand	131-135	5	8
α-helix	137-152	16
α-helix	154-158	5
α-helix	161-182	22
β-strand	185-189	5	8
β-strand	192-195	4	9
β-strand	233-236	4	9
α-helix	249-252	4
β-strand	258-260	3	8
β-strand	264-266	3	10
β-strand	305-307	3	10
β-strand	308-313	6	8
β-strand	338-344	7	8
β-strand	351-353	3	8

Chain B: 24 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	16-19	4
α-helix	25-27	3
α-helix	29-31	3
α-helix	32-41	10
α-helix	45-50	6
α-helix	53-60	8
α-helix	64-87	24
β-strand	90	1	8
β-strand	99-100	2	11
α-helix	105-111	7
β-strand	115-116	2	11
β-strand	120-125	6	2
α-helix	131-141	11
β-strand	154-159	6	2
α-helix	166-174	9
α-helix	177-182	6
α-helix	186-188	3
β-strand	189-193	5	2
α-helix	197-202	6
α-helix	203-207	5
α-helix	208-214	7
β-strand	219-224	6	2
α-helix	228-234	7
α-helix	242-264	23
β-strand	267-273	7	2
β-strand	274-276	3	12
α-helix	287-289	3
β-strand	292	1	9
α-helix	293-301	9
α-helix	305-317	13
α-helix	323-327	5
α-helix	331-338	8
α-helix	379-382	4
β-strand	384-386	3	12
α-helix	389-395	7
β-strand	396-406	11	2
β-strand	431-440	10	2
β-strand	446-453	8	2
β-strand	456-459	4	2

Chain C: 9 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	9-13	5	6
α-helix	17-28	12
β-strand	36-41	6	6
α-helix	48-54	7
α-helix	63-67	5
β-strand	71-73	3	6
α-helix	77-95	19
β-strand	110-117	8	6
α-helix	119-129	11
α-helix	132-151	20
β-strand	157-165	9	6
α-helix	167-170	4
α-helix	171-176	6
α-helix	199-206	8
β-strand	210-211	2	6

Chain D: 13 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	10-11	2	13
α-helix	12-14	3
β-strand	18	1	14
α-helix	19-21	3
α-helix	36-40	5
β-strand	43-48	6	20
α-helix	53-54	2
α-helix	55-61	7
β-strand	69-74	6	20
β-strand	90-92	3	20
α-helix	95-98	4
α-helix	100-112	13
α-helix	114-120	7
β-strand	130-136	7	20
α-helix	138-140	3
α-helix	157-171	15
β-strand	174-179	6	20
α-helix	184-186	3
α-helix	188-190	3
α-helix	213-217	5
β-strand	221-227	7	20
β-strand	232-236	5	20

Chain E: 7 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	3-11	9
β-strand	24-27	4	13
α-helix	31-37	7
β-strand	48	1	14
α-helix	51-59	9
β-strand	61-64	4	13
α-helix	69-81	13
β-strand	90-94	5	13
α-helix	96-99	4
α-helix	105-120	16
β-strand	125-129	5	13
α-helix	137-148	12

Chain F: 11 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	8-14	7
α-helix	26-35	10
α-helix	41-48	8
β-strand	53-54	2	15
β-strand	57-58	2	16
α-helix	72-79	8
β-strand	94-95	2	15
α-helix	103-104	2
β-strand	105-106	2	15
β-strand	107-108	2	17
β-strand	113-114	2	17
α-helix	117-128	12
α-helix	136-139	4
β-strand	141	1	18
β-strand	158	1	19
β-strand	167	1	19
β-strand	169	1	18
α-helix	177-186	10
α-helix	190-194	5
α-helix	195-199	5
β-strand	203-204	2	15
β-strand	207-208	2	16
α-helix	211-216	6

Chain G: 17 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	82	1	1
α-helix	83-85	3
α-helix	93-101	9
β-strand	106	1	1
α-helix	107-112	6
α-helix	115-120	6
α-helix	126-139	14
β-strand	145-146	2	2
α-helix	147-153	7
β-strand	159-160	2	3
α-helix	165-171	7
β-strand	175-176	2	3
β-strand	180-185	6	4
α-helix	191-201	11
α-helix	206-208	3
β-strand	214-219	6	4
α-helix	226-236	11
α-helix	240-245	6
β-strand	247-251	5	4
α-helix	255-271	17
β-strand	274-280	7	4
α-helix	282-289	8
α-helix	296-317	22
β-strand	320-326	7	4
β-strand	327-328	2	5
β-strand	343-344	2	5
α-helix	347-353	7
β-strand	356-362	7	4
β-strand	367-374	8	4
β-strand	382-388	7	4
β-strand	391-393	3	4
α-helix	394-396	3
α-helix	397-399	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA repair protein RAD51 homolog	G	protein	418	Saccharomyces cerevisiae AWRI1631	B5VHM3 (AlphaFold model)
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)
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
Platinum sensitivity protein 3	D	protein	281	Saccharomyces cerevisiae	Q12318
Chromosome segregation in meiosis protein 2	C	protein	213	Saccharomyces cerevisiae	P40465
ssDNA (8-mer)	H	DNA	9	synthetic construct

Sequence of entity 1 (G), FASTA

>9Q2C_1 DNA repair protein RAD51 homolog (chains G)
MHHHHHHHHGENLYFQGSMSQVQEQHISESQLQYGNGSLMSTVPADLSQSVVDGNGNGSS
EDIEATNGSGDGGGLQEQAEAQGEMEDEAYDEAALGSFVPIEKLQVNGITMADVKKLRES
GLHTAEAVAYAPRKDLLEIKGISEAKADKLLNEAARLVPMGFVTAADFHMRRSELICLTT
GSKNLDTLLGGGVETGSITELFGEFRTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEG
TFRPVRLVSIAQRFGLDPDDALNNVAYARAYNADHQLRLLDAAAQMMSESRFSLIVVDSV
MALYRTDFSGRGELSARQMHLAKFMRALQRLADQFGVAVVVTNQVVAQVDGGMAFNPDPK
KPIGGNIMAHSSTTRLGFKKGKGCQRLCKVVDSPCLPEAECVFAIYEDGVGDPREEDE

Sequence of entity 2 (A), FASTA

>9Q2C_2 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 3 (B), FASTA

>9Q2C_3 DNA repair protein RAD57 (chains B)
MPRALSIKFDNTYMDLYDELPESKLLYDEEFSYLLDAVRQNGVCVVDFLTLTPKELARLI
QRSINEVFRFQQLLVHEYNEKYLEICEKNSISPDNGPECFTTADVAMDELLGGGIFTHGI
TEIFGESSTGKSQLLMQLALSVQLSEPAGGLGGKCVYITTEGDLPTQRLESMLSSRPAYE
KLGITQSNIFTVSCNDLINQEHIINVQLPILLERSKGSIKLVIIDSISHHLRVELQNKSF
RESQENKNYLDRMAEKLQILAHDYSLSVVVANQVGDKPLANSPVAHRTYVTDYDYQLGWL
VGWKNSTILYRQMNSLLGASSNNDEILSDDEDYMLIERVMSTVNDRNYDFFSKKKPPIIE
NKTVERNSSSPISRQSKKRKFDYRVPNLGLTWSNHVSTRILLQKSFKASTIIQRGEAHLY
KGGDSASFWQVKRTMKVVYSTFAKPGQIAYQITKRGIETA

Sequence of entity 4 (E), FASTA

>9Q2C_4 Suppressor of HU sensitivity involved in recombination protein 1 (chains E)
MQFEERLQQLVESDWSLDQSSPNVLVIVLGDTARKYVELGGLKEHVTTNTVAGHVASRER
VSVVFLGRVKYLYMYLTRMQAQANGPQYSNVLVYGLWDLTATQDGPQQLRLLSLVLRQCL
SLPSKVEFYPEPPSSSVPARLLRFWDHIIR

Sequence of entity 5 (F), FASTA

>9Q2C_5 Suppressor of hydroxyurea sensitivity protein 2 (chains F)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGENLYFQGSKDVIEYSKLFAKLVNTNDD
TKLDDTIASFLYYMFPRELFIRAISLLESSDMFIYILDRVHNKEGNEHTSLIDVLVDEFY
KGSSNSLLEYRLIVKDTNDGAPPILVDIAHWFCSCEEFCKYFHEALEKTDEKEELHDVLI
NEVDDHLQFSDDRFAQLDPHSLSKQWYFKFDKVCCSHLLAFSILLRSSINVLKFFTVNSN
KVFVIAIDNIDEWLNLHINIVE

Sequence of entity 6 (D), FASTA

>9Q2C_6 Platinum sensitivity protein 3 (chains D)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGENLYFQMEVLKNIRIYPLSNFITSTKN
YINLPNELRNLISEEQESKLGFLHIIESDFKPSVALQKLVNCTTGDEKILIIDIVSIWSQ
QKQRQHGAIYMNSLSCINITGLIVFLELLYDSPMDALRRCQVDNFNFQLRGIVIDNLSFL
NFESDKNYDVINLSKFEKLFKILRKLREFLGCWIITKSFPTDFYNGIENTLVDKWSIKRK
SGVTLYPTKLPDSYMKGMDLIIYREVVDGRPQYRRIAALEE

Sequence of entity 7 (C), FASTA

>9Q2C_7 Chromosome segregation in meiosis protein 2 (chains C)
MEYEDLELITIWPSPTKNKLCQFIKQNLSKEHVVTQLFFIDATSSFPLSQFQKLVPPTLP
ENVRIYENIRINTCLDLEELSAITVKLLQILSMNKINAQRGTEDAVTEPLKIILYINGLE
VMFRNSQFKSSPQRSHELLRDTLLKLRVMGNDENENASIRTLLEFPKEQLLDYYLKKNNN
TRTSSVRSKRRRIKNGDSLAEYIWKYYADSLFE

Sequence of entity 8 (H), FASTA

>9Q2C_8 ssDNA (8-mer) (chains H)
TTTTTTTTT

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1
ZN	Zinc ion	Zn	1
MG	Magnesium ion	Mg	2
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	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

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