Histone-lysine N-methyltransferase 2C
Intermolecular
Cysteine 1057 and cysteine 1060
Cysteine 1057 and cysteine 1057
Cysteine 1060 and cysteine 1060
Cysteine 1078 and cysteine 1078
Cysteine 1057 and cysteine 1069
Cysteine 1136 and cysteine 1136
Cysteine 1081 and cysteine 1081
Cysteine 1069 and cysteine 1060
Cysteine 1060 and cysteine 1081
Cysteine 1057 and cysteine 1078
More...Intramolecular
Cysteine 4899 and cysteine 4906
Cysteine 4901 and cysteine 4906
Cysteine 4899 and cysteine 4901
Cysteine 4851 and cysteine 4906
Cysteine 4851 and cysteine 4901
Cysteine 1133 and cysteine 1136
Cysteine 4851 and cysteine 4899
Cysteine 1106 and cysteine 1136
Cysteine 1087 and cysteine 1090
Cysteine 1103 and cysteine 1136
Cysteine 1103 and cysteine 1133
Cysteine 1090 and cysteine 1114
Cysteine 1069 and cysteine 1078
Cysteine 1106 and cysteine 1133
Cysteine 1087 and cysteine 1114
Cysteine 1069 and cysteine 1081
Cysteine 1078 and cysteine 1081
Cysteine 1103 and cysteine 1106
Cysteine 4883 and cysteine 4901
Cysteine 1057 and cysteine 1081
Cysteine 4883 and cysteine 4906
Cysteine 4855 and cysteine 4883
Cysteine 1087 and cysteine 1133
Cysteine 4851 and cysteine 4883
Cysteine 4883 and cysteine 4899
6mlc A 1057 B 1060
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1057 and 1060.
Details
Redox score ?
75
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1057
Peptide B residue number
1060
Ligandability
Cysteine 1057 of Histone-lysine N-methyltransferase 2C
Cysteine 1060 of Histone-lysine N-methyltransferase 2C
6mlc A 1057 B 1057
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1057 and 1057.
Details
Redox score ?
74
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1057
Peptide B residue number
1057
Ligandability
6mlc A 1060 B 1060
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1060 and 1060.
Details
Redox score ?
73
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1060
Peptide B residue number
1060
Ligandability
6mlc A 1078 B 1078
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1078 and 1078.
Details
Redox score ?
61
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1078
Peptide B residue number
1078
Ligandability
6mlc A 1057 B 1069
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1057 and 1069. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1057
Peptide B residue number
1069
Ligandability
Cysteine 1057 of Histone-lysine N-methyltransferase 2C
Cysteine 1069 of Histone-lysine N-methyltransferase 2C
6mlc C 1136 D 1136
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1136 and 1136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1136
Peptide B residue number
1136
Ligandability
6mlc C 1081 D 1081
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1081 and 1081. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1081
Peptide B residue number
1081
Ligandability
6mlc A 1069 B 1060
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1069 and 1060. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1069
Peptide B residue number
1060
Ligandability
Cysteine 1069 of Histone-lysine N-methyltransferase 2C
Cysteine 1060 of Histone-lysine N-methyltransferase 2C
6mlc C 1060 D 1081
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1060 and 1081. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1060
Peptide B residue number
1081
Ligandability
Cysteine 1060 of Histone-lysine N-methyltransferase 2C
Cysteine 1081 of Histone-lysine N-methyltransferase 2C
6mlc A 1057 B 1078
A redox-regulated disulphide may form between two units of Histone-lysine N-methyltransferase 2C at cysteines 1057 and 1078. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide A name
Histone-lysine N-methyltransferase 2C
Peptide B name
Histone-lysine N-methyltransferase 2C
Peptide A accession
Q8NEZ4
Peptide B accession
Q8NEZ4
Peptide A residue number
1057
Peptide B residue number
1078
Ligandability
Cysteine 1057 of Histone-lysine N-methyltransferase 2C
Cysteine 1078 of Histone-lysine N-methyltransferase 2C
5f6k E 4899 E 4906
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4899 and 4906.
Details
Redox score ?
88
PDB code
5f6k
Structure name
crystal structure of the mll3-ash2l-rbbp5 complex
Structure deposition date
2015-12-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
4
Peptide accession
Q8NEZ4
Residue number A
4899
Residue number B
4906
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4899 of Histone-lysine N-methyltransferase 2C
Cysteine 4906 of Histone-lysine N-methyltransferase 2C
5f6k E 4901 E 4906
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4901 and 4906.
Details
Redox score ?
88
PDB code
5f6k
Structure name
crystal structure of the mll3-ash2l-rbbp5 complex
Structure deposition date
2015-12-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
8
Peptide accession
Q8NEZ4
Residue number A
4901
Residue number B
4906
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4901 of Histone-lysine N-methyltransferase 2C
Cysteine 4906 of Histone-lysine N-methyltransferase 2C
5f6k E 4899 E 4901
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4899 and 4901.
Details
Redox score ?
87
PDB code
5f6k
Structure name
crystal structure of the mll3-ash2l-rbbp5 complex
Structure deposition date
2015-12-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
12
Peptide accession
Q8NEZ4
Residue number A
4899
Residue number B
4901
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4899 of Histone-lysine N-methyltransferase 2C
Cysteine 4901 of Histone-lysine N-methyltransferase 2C
7w6l E 4851 E 4906
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4851 and 4906.
Details
Redox score ?
84
PDB code
7w6l
Structure name
the crystal structure of mll3-rbbp5-ash2l in complex with h3k4me0 peptide
Structure deposition date
2021-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
4
Peptide accession
Q8NEZ4
Residue number A
4851
Residue number B
4906
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4851 of Histone-lysine N-methyltransferase 2C
Cysteine 4906 of Histone-lysine N-methyltransferase 2C
5f6k C 4851 C 4901
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4851 and 4901.
Details
Redox score ?
83
PDB code
5f6k
Structure name
crystal structure of the mll3-ash2l-rbbp5 complex
Structure deposition date
2015-12-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
16
Peptide accession
Q8NEZ4
Residue number A
4851
Residue number B
4901
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4851 of Histone-lysine N-methyltransferase 2C
Cysteine 4901 of Histone-lysine N-methyltransferase 2C
6mlc D 1133 D 1136
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1133 and 1136.
Details
Redox score ?
79
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1133
Residue number B
1136
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1133 of Histone-lysine N-methyltransferase 2C
Cysteine 1136 of Histone-lysine N-methyltransferase 2C
7w6l C 4851 C 4899
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4851 and 4899.
Details
Redox score ?
77
PDB code
7w6l
Structure name
the crystal structure of mll3-rbbp5-ash2l in complex with h3k4me0 peptide
Structure deposition date
2021-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
25
Peptide accession
Q8NEZ4
Residue number A
4851
Residue number B
4899
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4851 of Histone-lysine N-methyltransferase 2C
Cysteine 4899 of Histone-lysine N-methyltransferase 2C
6mlc C 1106 C 1136
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1106 and 1136.
Details
Redox score ?
76
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1106
Residue number B
1136
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1106 of Histone-lysine N-methyltransferase 2C
Cysteine 1136 of Histone-lysine N-methyltransferase 2C
6mlc A 1087 A 1090
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1087 and 1090.
Details
Redox score ?
75
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1087
Residue number B
1090
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1087 of Histone-lysine N-methyltransferase 2C
Cysteine 1090 of Histone-lysine N-methyltransferase 2C
6mlc B 1103 B 1136
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1103 and 1136.
Details
Redox score ?
75
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1103
Residue number B
1136
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1103 of Histone-lysine N-methyltransferase 2C
Cysteine 1136 of Histone-lysine N-methyltransferase 2C
6mlc B 1103 B 1133
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1103 and 1133.
Details
Redox score ?
75
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1103
Residue number B
1133
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1103 of Histone-lysine N-methyltransferase 2C
Cysteine 1133 of Histone-lysine N-methyltransferase 2C
6mlc B 1090 B 1114
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1090 and 1114.
Details
Redox score ?
75
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1090
Residue number B
1114
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1090 of Histone-lysine N-methyltransferase 2C
Cysteine 1114 of Histone-lysine N-methyltransferase 2C
6mlc A 1069 A 1078
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1069 and 1078.
Details
Redox score ?
75
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1069
Residue number B
1078
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1069 of Histone-lysine N-methyltransferase 2C
Cysteine 1078 of Histone-lysine N-methyltransferase 2C
6mlc C 1106 C 1133
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1106 and 1133.
Details
Redox score ?
74
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1106
Residue number B
1133
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1106 of Histone-lysine N-methyltransferase 2C
Cysteine 1133 of Histone-lysine N-methyltransferase 2C
6mlc A 1087 A 1114
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1087 and 1114.
Details
Redox score ?
73
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1087
Residue number B
1114
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1087 of Histone-lysine N-methyltransferase 2C
Cysteine 1114 of Histone-lysine N-methyltransferase 2C
6mlc D 1069 D 1081
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1069 and 1081.
Details
Redox score ?
73
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1069
Residue number B
1081
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1069 of Histone-lysine N-methyltransferase 2C
Cysteine 1081 of Histone-lysine N-methyltransferase 2C
6mlc B 1078 B 1081
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1078 and 1081.
Details
Redox score ?
73
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1078
Residue number B
1081
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1078 of Histone-lysine N-methyltransferase 2C
Cysteine 1081 of Histone-lysine N-methyltransferase 2C
6mlc A 1103 A 1106
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1103 and 1106.
Details
Redox score ?
71
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1103
Residue number B
1106
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1103 of Histone-lysine N-methyltransferase 2C
Cysteine 1106 of Histone-lysine N-methyltransferase 2C
5f6k C 4883 C 4901
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4883 and 4901. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
5f6k
Structure name
crystal structure of the mll3-ash2l-rbbp5 complex
Structure deposition date
2015-12-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
5
% buried
54
Peptide accession
Q8NEZ4
Residue number A
4883
Residue number B
4901
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4883 of Histone-lysine N-methyltransferase 2C
Cysteine 4901 of Histone-lysine N-methyltransferase 2C
6mlc B 1057 B 1081
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1057 and 1081. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1057
Residue number B
1081
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1057 of Histone-lysine N-methyltransferase 2C
Cysteine 1081 of Histone-lysine N-methyltransferase 2C
6kiw K 4883 K 4906
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4883 and 4906. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6kiw
Structure name
cryo-em structure of human mll3-ubncp complex (4
Structure deposition date
2019-07-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
30
Peptide accession
Q8NEZ4
Residue number A
4883
Residue number B
4906
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4883 of Histone-lysine N-methyltransferase 2C
Cysteine 4906 of Histone-lysine N-methyltransferase 2C
5f6k E 4855 E 4883
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4855 and 4883. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5f6k
Structure name
crystal structure of the mll3-ash2l-rbbp5 complex
Structure deposition date
2015-12-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
78
Peptide accession
Q8NEZ4
Residue number A
4855
Residue number B
4883
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4855 of Histone-lysine N-methyltransferase 2C
Cysteine 4883 of Histone-lysine N-methyltransferase 2C
6mlc A 1087 A 1133
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 1087 and 1133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6mlc
Structure name
phd6 domain of mll3 in complex with histone h4
Structure deposition date
2018-09-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NEZ4
Residue number A
1087
Residue number B
1133
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 1087 of Histone-lysine N-methyltransferase 2C
Cysteine 1133 of Histone-lysine N-methyltransferase 2C
5f6k E 4851 E 4883
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4851 and 4883. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5f6k
Structure name
crystal structure of the mll3-ash2l-rbbp5 complex
Structure deposition date
2015-12-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
38
Peptide accession
Q8NEZ4
Residue number A
4851
Residue number B
4883
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4851 of Histone-lysine N-methyltransferase 2C
Cysteine 4883 of Histone-lysine N-methyltransferase 2C
7w6l C 4883 C 4899
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase 2C between cysteines 4883 and 4899. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7w6l
Structure name
the crystal structure of mll3-rbbp5-ash2l in complex with h3k4me0 peptide
Structure deposition date
2021-12-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
60
Peptide accession
Q8NEZ4
Residue number A
4883
Residue number B
4899
Peptide name
Histone-lysine N-methyltransferase 2C
Ligandability
Cysteine 4883 of Histone-lysine N-methyltransferase 2C
Cysteine 4899 of Histone-lysine N-methyltransferase 2C
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