Histone-lysine N-methyltransferase KMT5C
Intramolecular
Cysteine 185 and cysteine 234
Cysteine 229 and cysteine 234
Cysteine 231 and cysteine 234
Cysteine 229 and cysteine 231
Cysteine 185 and cysteine 229
Cysteine 185 and cysteine 231
Cysteine 95 and cysteine 141
Cysteine 189 and cysteine 215
Cysteine 189 and cysteine 200
3rq4 A 185 A 234
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 185 and 234.
Details
Redox score ?
75
PDB code
3rq4
Structure name
crystal structure of suppressor of variegation 4-20 homolog 2
Structure deposition date
2011-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q86Y97
Residue number A
185
Residue number B
234
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 185 of Histone-lysine N-methyltransferase KMT5C
Cysteine 234 of Histone-lysine N-methyltransferase KMT5C
3rq4 A 229 A 234
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 229 and 234.
Details
Redox score ?
75
PDB code
3rq4
Structure name
crystal structure of suppressor of variegation 4-20 homolog 2
Structure deposition date
2011-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q86Y97
Residue number A
229
Residue number B
234
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 229 of Histone-lysine N-methyltransferase KMT5C
Cysteine 234 of Histone-lysine N-methyltransferase KMT5C
3rq4 A 231 A 234
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 231 and 234.
Details
Redox score ?
75
PDB code
3rq4
Structure name
crystal structure of suppressor of variegation 4-20 homolog 2
Structure deposition date
2011-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q86Y97
Residue number A
231
Residue number B
234
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 231 of Histone-lysine N-methyltransferase KMT5C
Cysteine 234 of Histone-lysine N-methyltransferase KMT5C
3rq4 A 229 A 231
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 229 and 231.
Details
Redox score ?
74
PDB code
3rq4
Structure name
crystal structure of suppressor of variegation 4-20 homolog 2
Structure deposition date
2011-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q86Y97
Residue number A
229
Residue number B
231
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 229 of Histone-lysine N-methyltransferase KMT5C
Cysteine 231 of Histone-lysine N-methyltransferase KMT5C
3rq4 A 185 A 229
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 185 and 229.
Details
Redox score ?
74
PDB code
3rq4
Structure name
crystal structure of suppressor of variegation 4-20 homolog 2
Structure deposition date
2011-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q86Y97
Residue number A
185
Residue number B
229
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 185 of Histone-lysine N-methyltransferase KMT5C
Cysteine 229 of Histone-lysine N-methyltransferase KMT5C
3rq4 A 185 A 231
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 185 and 231.
Details
Redox score ?
72
PDB code
3rq4
Structure name
crystal structure of suppressor of variegation 4-20 homolog 2
Structure deposition date
2011-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q86Y97
Residue number A
185
Residue number B
231
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 185 of Histone-lysine N-methyltransferase KMT5C
Cysteine 231 of Histone-lysine N-methyltransferase KMT5C
4au7 B 95 B 141
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 95 and 141.
Details
Redox score ?
65
PDB code
4au7
Structure name
the structure of the suv4-20h2 ternary complex with histone h4
Structure deposition date
2012-05-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
95
Peptide accession
Q6Q783
Residue number A
95
Residue number B
141
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 95 of Histone-lysine N-methyltransferase KMT5C
Cysteine 141 of Histone-lysine N-methyltransferase KMT5C
3rq4 A 189 A 215
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 189 and 215.
Details
Redox score ?
63
PDB code
3rq4
Structure name
crystal structure of suppressor of variegation 4-20 homolog 2
Structure deposition date
2011-04-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q86Y97
Residue number A
189
Residue number B
215
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 189 of Histone-lysine N-methyltransferase KMT5C
Cysteine 215 of Histone-lysine N-methyltransferase KMT5C
4au7 B 189 B 200
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5C between cysteines 189 and 200. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4au7
Structure name
the structure of the suv4-20h2 ternary complex with histone h4
Structure deposition date
2012-05-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
54
Peptide accession
Q6Q783
Residue number A
189
Residue number B
200
Peptide name
Histone-lysine N-methyltransferase KMT5C
Ligandability
Cysteine 189 of Histone-lysine N-methyltransferase KMT5C
Cysteine 200 of Histone-lysine N-methyltransferase KMT5C
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