6J0W: Yeast Rtt107 and Nse6

Crystal Structure of Yeast Rtt107 and Nse6. Determined by X-ray diffraction at 2.4 Å resolution. Released 14 Aug 2019.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 4
Atoms: 7,963
Mol. weight: 125.04 kDa
Released: 14 Aug 2019

Explore 6J0W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6J0W contains 60 α-helices and 48 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: 29 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	11-16	6	1
α-helix	19-21	3
α-helix	22-34	13
β-strand	39-44	6	1
α-helix	57-64	8
α-helix	68-69	2
β-strand	71-73	3	1
α-helix	82-83	2
α-helix	84-88	5
β-strand	93-94	2	1
α-helix	96-105	10
α-helix	112-114	3
β-strand	126-129	4	2
α-helix	131-133	3
α-helix	136-148	13
β-strand	152-154	3	2
β-strand	157-158	2	3
β-strand	163-165	3	2
α-helix	172-177	6
β-strand	202-204	3	2
α-helix	207-215	9
α-helix	223-226	4
β-strand	228	1	2
α-helix	236-247	12
β-strand	270-273	4	4
α-helix	274	1
α-helix	281-293	13
β-strand	297-300	4	4
α-helix	307-313	7
β-strand	319-321	3	4
β-strand	324	1	5
α-helix	328-336	9
β-strand	341-343	3	4
α-helix	345-354	10
α-helix	360-362	3
α-helix	365-367	3
α-helix	369	1
β-strand	370	1	5
α-helix	371-373	3
β-strand	381-384	4	6
α-helix	390-402	13
β-strand	405-407	3	6
β-strand	410	1	7
β-strand	416-418	3	6
α-helix	425-433	9
β-strand	442-444	3	6
α-helix	446-455	10
α-helix	465-467	3
α-helix	471-473	3
α-helix	475-477	3

Chain B: 30 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	11-16	6	8
α-helix	19-21	3
α-helix	22-34	13
β-strand	39-44	6	8
α-helix	45-47	3
β-strand	50	1	9
β-strand	53	1	9
α-helix	57-64	8
β-strand	72-73	2	8
α-helix	82-83	2
α-helix	84-88	5
β-strand	93-94	2	8
α-helix	96-105	10
α-helix	112-114	3
β-strand	126-129	4	10
α-helix	131-133	3
α-helix	136-148	13
α-helix	151	1
β-strand	152-154	3	10
β-strand	157	1	11
β-strand	163-165	3	10
α-helix	173-177	5
β-strand	202-204	3	10
α-helix	207-215	9
α-helix	222-227	6
β-strand	228	1	10
α-helix	236-246	11
β-strand	270-273	4	12
α-helix	281-293	13
β-strand	297-300	4	12
α-helix	307-313	7
β-strand	319-321	3	12
β-strand	324	1	13
α-helix	328-336	9
β-strand	341-343	3	12
α-helix	345-354	10
α-helix	360-362	3
α-helix	365-367	3
α-helix	369	1
β-strand	370	1	13
α-helix	371-373	3
α-helix	377-379	3
β-strand	381-384	4	14
α-helix	390-402	13
β-strand	405-406	2	14
β-strand	410	1	15
β-strand	416-419	4	14
α-helix	425-434	10
β-strand	442-445	4	14
α-helix	446-455	10
α-helix	464-466	3
α-helix	471-473	3
α-helix	475-477	3

Chain C: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	15	1	7
β-strand	26-28	3	3

Chain D: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	15	1	15
α-helix	16-17	2
β-strand	28	1	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Regulator of Ty1 transposition protein 107	A, B	protein	513	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P38850 (AlphaFold model)
Peptide from DNA repair protein KRE29	C, D	protein	29	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P40026 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6J0W_1 Regulator of Ty1 transposition protein 107 (chains A, B)
MSTSLLFEQLNFLILVAAEAELPIAHSTRKLLMDNSCNNCQIYELYNENLKDVKTDKDWF
MNKFGPQTVHFVISNTINFPFYKIVYFDLLIPVVSHTWVQDSVKTKRHLRTNMYSPNPFH
LLRDCQVYISKSSFNKCEYILYSDLLHLLGGTLVNYISNRTTHVIVQSPQDPIIATVSKL
TFGSFSSSSTNKHTEKPLREWKFVYPIWILYHFKMAKPLKGELATLCELDMQDTSEEQLF
AKWEEVIGDKQTSSSQLTLHPNKTLFKNHHFAISPDLNFFTPLYWFLKGFIEDLDGKVTP
LSFSDDLKSVYQAFPDIDCYIGHSANSPILEKTKSIKPEIHVGNVSWLFYMFALQKFTPV
SQCKLIHQPFHAKLFTSKELTVAYTNYFGSQRFYIQRLVEILGGLSTPELTRKNTHLITK
STIGKKFKVAKKWSLDPQNAIIVTNHMWLEQCYMNNSKLNPKDSRFQNFKLDDNMGWNIG
QIGMDHSSLPTPKNLSMVTYDTQSISEKPPPTN

Sequence of entity 2 (C, D), FASTA

>6J0W_2 Peptide from DNA repair protein KRE29 (chains C, D)
ETVPDSQISGFDSPLIPTSVGSYFRDDDD

Primary citation

Molecular Basis for Control of Diverse Genome Stability Factors by the Multi-BRCT Scaffold Rtt107. Wan, B., Wu, J., Meng, X. et al. Mol Cell (2019) 75:238-251.e5. DOI 10.1016/j.molcel.2019.05.035 · PubMed

Other PDB entries of the same protein (UniProt P38850 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6J0Y 1.8 Å, Crystal Structure of Yeast Rtt107 and Slx4
3T7K 2.03 Å, Complex structure of Rtt107p and phosphorylated histone H2A
3T7J 2.04 Å, Crystal structure of Rtt107p (residues 820-1070)
3T7I 2.3 Å, Crystal structure of Se-Met Rtt107p (residues 820-1070)
6J0X 2.31 Å, Crystal Structure of Yeast Rtt107 and Mms22
6J0V 2.31 Å, Crystal Structure of Yeast Rtt107

Browse structure collections

About this viewer

MolViewer shows 6J0W 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.