5XYN: Csm2-Psy3-Shu1-Shu2 complex from budding yeast

The crystal structure of Csm2-Psy3-Shu1-Shu2 complex from budding yeast. Determined by X-ray diffraction at 3.3 Å resolution. Released 8 Nov 2017.

Method: X-ray diffraction
Resolution: 3.3 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 4
Atoms: 6,028
Mol. weight: 96.77 kDa
Ligands: ZN
Released: 8 Nov 2017

Explore 5XYN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5XYN contains 46 α-helices and 30 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.

Chain A: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	0-5	6
β-strand	9-11	3	1
α-helix	12-15	4
β-strand	17-18	2	2
α-helix	27-32	6
α-helix	35-38	4
β-strand	43-47	5	3
α-helix	53-54	2
α-helix	55-61	7
β-strand	69-74	6	3
α-helix	82-84	3
β-strand	89-92	4	3
α-helix	95-97	3
α-helix	100-112	13
α-helix	114-119	6
β-strand	129	1	4
β-strand	130-136	7	3
α-helix	138-140	3
α-helix	157-171	15
β-strand	174-179	6	3
α-helix	182-186	5
α-helix	188-190	3
α-helix	213-218	6
β-strand	221-226	6	3
β-strand	233-236	4	3

Chain B: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
β-strand	9-13	5	5
α-helix	17-28	12
β-strand	34-41	8	5
α-helix	48-54	7
α-helix	60-62	3
α-helix	63-67	5
β-strand	69-73	5	5
α-helix	77-95	19
α-helix	108-109	2
β-strand	110-117	8	5
α-helix	119-129	11
α-helix	132-151	20
β-strand	157-165	9	5
α-helix	171-176	6
α-helix	199-206	8
β-strand	210-211	2	5

Chain C: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	3-11	9
α-helix	14-15	2
β-strand	24-29	6	1
α-helix	31-38	8
β-strand	47-48	2	2
β-strand	50	1	4
α-helix	51-55	5
α-helix	56-60	5
β-strand	61-66	6	1
α-helix	69-81	13
β-strand	90-94	5	1
α-helix	96-99	4
α-helix	105-119	15
β-strand	125-129	5	1
α-helix	131-133	3
α-helix	137-149	13

Chain D: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	8-13	6
α-helix	26-35	10
α-helix	40-49	10
β-strand	53-57	5	6
α-helix	72-81	10
β-strand	91-95	5	6
β-strand	105-108	4	6
β-strand	113-114	2	6
α-helix	117-128	12
α-helix	136-140	5
β-strand	141-144	4	7
α-helix	147-149	3
β-strand	157-158	2	7
β-strand	166-169	4	7
α-helix	177-186	10
α-helix	190-195	6
β-strand	203-207	5	6
α-helix	211-217	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Platinum sensitivity protein 3	A	protein	244	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	Q12318 (AlphaFold model)
Chromosome segregation in meiosis protein 2	B	protein	213	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P40465 (AlphaFold model)
Suppressor of HU sensitivity involved in recombination protein 1	C	protein	150	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P38751 (AlphaFold model)
Suppressor of hydroxyurea sensitivity protein 2	D	protein	223	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P38957 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5XYN_1 Platinum sensitivity protein 3 (chains A)
GSMEVLKNIRIYPLSNFITSTKNYINLPNELRNLISEEQESKLGFLHIIESDFKPSVALQ
KLVNCTTGDEKILIIDIVSIWSQQKQRQHGAIYMNSLSCINITGLIVFLELLYDSPMDAL
RRCQVDNFNFQLRGIVIDNLSFLNFESDKNYDVINLSKFEKLFKILRKLREFLGCWIITK
SFPTDFYNGIENTLVDKWSIKRKSGVTLYPTKLPDSYMKGMDLIIYREVVDGRPQYRRIA
ALEE

Sequence of entity 2 (B), FASTA

>5XYN_2 Chromosome segregation in meiosis protein 2 (chains B)
MEYEDLELITIWPSPTKNKLCQFIKQNLSKEHVVTQLFFIDATSSFPLSQFQKLVPPTLP
ENVRIYENIRINTCLDLEELSAITVKLLQILSMNKINAQRGTEDAVTEPLKIILYINGLE
VMFRNSQFKSSPQRSHELLRDTLLKLRVMGNDENENASIRTLLEFPKEQLLDYYLKKNNN
TRTSSVRSKRRRIKNGDSLAEYIWKYYADSLFE

Sequence of entity 3 (C), FASTA

>5XYN_3 Suppressor of HU sensitivity involved in recombination protein 1 (chains C)
MQFEERLQQLVESDWSLDQSSPNVLVIVLGDTARKYVELGGLKEHVTTNTVAGHVASRER
VSVVFLGRVKYLYMYLTRMQAQANGPQYSNVLVYGLWDLTATQDGPQQLRLLSLVLRQCL
SLPSKVEFYPEPPSSSVPARLLRFWDHIIR

Sequence of entity 4 (D), FASTA

>5XYN_4 Suppressor of hydroxyurea sensitivity protein 2 (chains D)
MSKDVIEYSKLFAKLVNTNDDTKLDDTIASFLYYMFPRELFIRAISLLESSDMFIYILDR
VHNKEGNEHTSLIDVLVDEFYKGSSNSLLEYRLIVKDTNDGAPPILVDIAHWFCSCEEFC
KYFHEALEKTDEKEELHDVLINEVDDHLQFSDDRFAQLDPHSLSKQWYFKFDKVCCSHLL
AFSILLRSSINVLKFFTVNSNKVFVIAIDNIDEWLNLHINIVE

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

Structural basis for the functional role of the Shu complex in homologous recombination. Zhang, S., Wang, L., Tao, Y. et al. Nucleic Acids Res (2017) 45:13068-13079. DOI 10.1093/nar/gkx992 · PubMed

Other PDB entries of the same protein (UniProt Q12318 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3VU9 1.75 Å, Crystal Structure of Psy3-Csm2 complex
4EQ6 1.8 Å, The crystal structure of Psy3-Csm2 complex from budding yeast
4DT1 1.9 Å, Crystal structure of the Psy3-Csm2 complex
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
9Q2E 3.44 Å, Rad55-Rad57-SHU bound to ssDNA
9Q2L 3.7 Å, Rad55-Rad57(E161Q)-SHU-3xRad51 bound to ssDNA with ATP

Browse structure collections

About this viewer

MolViewer shows 5XYN directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.