6J0X: Yeast Rtt107 and Mms22

Crystal Structure of Yeast Rtt107 and Mms22. Determined by X-ray diffraction at 2.31 Å resolution. Released 14 Aug 2019.

Method: X-ray diffraction
Resolution: 2.31 Å
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 8
Atoms: 16,129
Mol. weight: 245.51 kDa
Released: 14 Aug 2019

Explore 6J0X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6J0X contains 120 α-helices and 88 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: 29 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	12-16	5	1
α-helix	19-21	3
α-helix	22-34	13
β-strand	40-44	5	1
α-helix	45-47	3
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	136-148	13
β-strand	152-153	2	2
β-strand	157-158	2	3
β-strand	163-165	3	2
α-helix	172-180	9
β-strand	202-204	3	2
α-helix	207-215	9
α-helix	221-226	6
β-strand	228	1	2
α-helix	236-247	12
α-helix	253-254	2
β-strand	270-273	4	4
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	381-385	5	6
α-helix	390-402	13
β-strand	405-406	2	6
β-strand	416-419	4	6
α-helix	425-433	9
β-strand	442-444	3	6
α-helix	447-455	9
α-helix	464-466	3
α-helix	471-473	3
α-helix	475-477	3

Chain B: 29 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	11-16	6	7
α-helix	19-21	3
α-helix	22-34	13
β-strand	39-44	6	7
α-helix	57-64	8
α-helix	68-69	2
β-strand	71-73	3	7
α-helix	82-83	2
α-helix	84-88	5
β-strand	93-94	2	7
α-helix	96-105	10
α-helix	112-114	3
β-strand	126-129	4	8
α-helix	136-148	13
β-strand	152-153	2	8
β-strand	157-158	2	9
β-strand	163-165	3	8
α-helix	172-178	7
β-strand	202-204	3	8
α-helix	207-215	9
α-helix	221-226	6
β-strand	228	1	8
α-helix	236-247	12
α-helix	253-254	2
β-strand	270-273	4	10
α-helix	274	1
α-helix	281-292	12
β-strand	297-300	4	10
α-helix	307-313	7
β-strand	317-321	5	10
β-strand	324	1	11
α-helix	328-336	9
β-strand	341-343	3	10
α-helix	345-354	10
α-helix	360-362	3
α-helix	365-367	3
α-helix	369	1
β-strand	370	1	11
α-helix	371-373	3
β-strand	381-385	5	12
α-helix	390-402	13
β-strand	405-406	2	12
β-strand	416-419	4	12
α-helix	425-433	9
β-strand	442-444	3	12
α-helix	446-454	9
α-helix	464-466	3
α-helix	471-473	3
α-helix	475-477	3

Chain C: 28 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8	1	13
β-strand	11-16	6	14
α-helix	19-21	3
α-helix	22-34	13
β-strand	37	1	13
β-strand	39-44	6	14
α-helix	57-64	8
α-helix	68-69	2
β-strand	71-73	3	14
α-helix	82-83	2
α-helix	84-88	5
β-strand	93-94	2	14
α-helix	97-105	9
α-helix	112-114	3
β-strand	126-129	4	15
α-helix	136-148	13
β-strand	152-153	2	15
β-strand	157-158	2	16
β-strand	163-165	3	15
α-helix	172-180	9
β-strand	202-204	3	15
α-helix	207-215	9
α-helix	222-226	5
β-strand	228	1	15
α-helix	236-247	12
α-helix	254-259	6
β-strand	270-273	4	17
α-helix	281-293	13
β-strand	297-300	4	17
α-helix	307-313	7
β-strand	317-321	5	17
β-strand	324	1	18
α-helix	328-336	9
β-strand	341-343	3	17
α-helix	345-354	10
α-helix	360-362	3
α-helix	365-367	3
α-helix	369	1
β-strand	370	1	18
α-helix	371-373	3
β-strand	381-385	5	19
α-helix	390-402	13
β-strand	405-406	2	19
β-strand	416-419	4	19
α-helix	425-433	9
β-strand	442-444	3	19
α-helix	446-455	10
α-helix	464-467	4
α-helix	471-473	3
α-helix	475-477	3

Chain D: 29 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8	1	20
β-strand	11-16	6	21
α-helix	19-21	3
α-helix	22-34	13
β-strand	37	1	20
β-strand	39-44	6	21
α-helix	57-64	8
α-helix	68-69	2
β-strand	71-73	3	21
α-helix	82-83	2
α-helix	84-88	5
β-strand	93-94	2	21
α-helix	97-105	9
α-helix	112-114	3
β-strand	126-129	4	22
α-helix	136-148	13
β-strand	152-153	2	22
β-strand	157-158	2	23
β-strand	163-165	3	22
α-helix	172-180	9
β-strand	202-204	3	22
α-helix	207-215	9
α-helix	222-226	5
β-strand	228	1	22
α-helix	236-247	12
β-strand	270-273	4	24
α-helix	274	1
α-helix	275-277	3
α-helix	281-293	13
β-strand	297-300	4	24
α-helix	307-313	7
β-strand	319-321	3	24
β-strand	324	1	25
α-helix	328-336	9
β-strand	341-343	3	24
α-helix	345-354	10
α-helix	360-362	3
α-helix	365-367	3
α-helix	369	1
β-strand	370	1	25
α-helix	371-372	2
β-strand	381-385	5	26
α-helix	390-402	13
β-strand	405-406	2	26
β-strand	416-419	4	26
α-helix	425-434	10
β-strand	442-444	3	26
α-helix	446-454	9
α-helix	464-466	3
α-helix	471-473	3
α-helix	475-477	3

Chain E: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	23-25	3	3
α-helix	27-29	3
α-helix	33-35	3

Chains F and H: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	23-25	3	9
α-helix	27-29	3

Chain G: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	23-25	3	16
α-helix	27-30	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Regulator of Ty1 transposition protein 107	A, B, C, D	protein	513	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P38850 (AlphaFold model)
Peptide from E3 ubiquitin-protein ligase substrate receptor MMS22	E, F, G, H	protein	16	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	Q06164 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>6J0X_1 Regulator of Ty1 transposition protein 107 (chains A, B, C, D)
MSTSLLFEQLNFLILVAAEAELPIAHSTRKLLMDNSCNNCQIYELYNENLKDVKTDKDWF
MNKFGPQTVHFVISNTINFPFYKIVYFDLLIPVVSHTWVQDSVKTKRHLRTNMYSPNPFH
LLRDCQVYISKSSFNKCEYILYSDLLHLLGGTLVNYISNRTTHVIVQSPQDPIIATVSKL
TFGSFSSSSTNKHTEKPLREWKFVYPIWILYHFKMAKPLKGELATLCELDMQDTSEEQLF
AKWEEVIGDKQTSSSQLTLHPNKTLFKNHHFAISPDLNFFTPLYWFLKGFIEDLDGKVTP
LSFSDDLKSVYQAFPDIDCYIGHSANSPILEKTKSIKPEIHVGNVSWLFYMFALQKFTPV
SQCKLIHQPFHAKLFTSKELTVAYTNYFGSQRFYIQRLVEILGGLSTPELTRKNTHLITK
STIGKKFKVAKKWSLDPQNAIIVTNHMWLEQCYMNNSKLNPKDSRFQNFKLDDNMGWNIG
QIGMDHSSLPTPKNLSMVTYDTQSISEKPPPTN

Sequence of entity 2 (E, F, G, H), FASTA

>6J0X_2 Peptide from E3 ubiquitin-protein ligase substrate receptor MMS22 (chains E, F, G, H)
SIIYEPEFNENYLWAE

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)
6J0V 2.31 Å, Crystal Structure of Yeast Rtt107
6J0W 2.4 Å, Crystal Structure of Yeast Rtt107 and Nse6

Browse structure collections

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