3T7I: Se-Met Rtt107p

Crystal structure of Se-Met Rtt107p (residues 820-1070). Determined by X-ray diffraction at 2.3 Å resolution. Released 15 Feb 2012.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 3,947
Mol. weight: 59.13 kDa
Released: 15 Feb 2012

Explore 3T7I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3T7I contains 28 α-helices and 20 β-strands across 2 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, 10 β-strands

Element	Residues	Length	Sheet
α-helix	821-826	6
β-strand	837-841	5	1
α-helix	851-859	9
β-strand	862-864	3	1
α-helix	870-872	3
β-strand	876-878	3	1
α-helix	886-891	6
β-strand	899-901	3	1
α-helix	904-913	10
α-helix	927-930	4
β-strand	931	1	1
α-helix	932	1
α-helix	937-940	4
α-helix	941-944	4
α-helix	949-952	4
β-strand	957-961	5	2
α-helix	967-977	11
β-strand	982-986	5	2
α-helix	993-995	3
β-strand	1012-1016	5	2
α-helix	1019-1032	14
β-strand	1038-1042	5	2
α-helix	1043-1051	9
β-strand	1063-1067	5	2

Chain B: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	821-827	7
β-strand	837-841	5	3
α-helix	851-859	9
β-strand	862-864	3	3
α-helix	870-872	3
β-strand	876-878	3	3
α-helix	886-891	6
β-strand	899-901	3	3
α-helix	904-913	10
α-helix	927-930	4
β-strand	931	1	3
α-helix	932	1
α-helix	937-942	6
α-helix	949-952	4
β-strand	957-961	5	4
α-helix	968-977	10
β-strand	982-986	5	4
α-helix	987	1
α-helix	993-995	3
β-strand	1012-1015	4	4
α-helix	1019-1032	14
β-strand	1038-1041	4	4
α-helix	1043-1052	10
β-strand	1063-1067	5	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Regulator of Ty1 transposition protein 107	A, B	protein	256	Saccharomyces cerevisiae	P38850 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3T7I_1 Regulator of Ty1 transposition protein 107 (chains A, B)
GSPHMTKAEKILARFNELPNYDLKAVCTGCFHDGFNEVDIEILNQLGIKIFDNIKETDKL
NCIFAPKILRTEKFLKSLSFEPLKFALKPEFIIDMLKQIHSKKDKLSQININLFDYEING
INESIISKTKLPTKVFERANIRCINLVNDIPGGVDTIGSVLKAHGIEKINVLRSKKCTFE
DIIPNDVSKQENGGIFKYVLIVTKASQVKKFTKMINDRDKNETILIVEWNWCVESIFHLN
VDFTSKKNVLYQKKNN

Primary citation

Structure of C-terminal Tandem BRCT Repeats of Rtt107 Protein Reveals Critical Role in Interaction with Phosphorylated Histone H2A during DNA Damage Repair. Li, X., Liu, K., Li, F. et al. J Biol Chem (2012) 287:9137-9146. DOI 10.1074/jbc.M111.311860 · 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)
6J0X 2.31 Å, Crystal Structure of Yeast Rtt107 and Mms22
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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