Set1/Ash2 histone methyltransferase complex subunit ASH2
Intermolecular
Cysteine 581 and cysteine 581
Intramolecular
Cysteine 147 and cysteine 150
Cysteine 117 and cysteine 150
Cysteine 117 and cysteine 147
Cysteine 117 and cysteine 120
Cysteine 120 and cysteine 150
Cysteine 120 and cysteine 147
Cysteine 136 and cysteine 207
3toj A 487 B 487
A redox-regulated disulphide may form between two units of Set1/Ash2 histone methyltransferase complex subunit ASH2 at cysteines 581 and 581 (487 and 487 respectively in this structure).
Details
Redox score ?
81
PDB code
3toj
Structure name
structure of the spry domain of human ash2l
Structure deposition date
2011-09-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide A name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Peptide B name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Peptide A accession
Q9UBL3
Peptide B accession
Q9UBL3
Peptide A residue number
581
Peptide B residue number
581
Ligandability
3s32 A 147 A 150
A redox-regulated disulphide may form within Set1/Ash2 histone methyltransferase complex subunit ASH2 between cysteines 147 and 150.
Details
Redox score ?
84
PDB code
3s32
Structure name
crystal structure of ash2l n-terminal domain
Structure deposition date
2011-05-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
2
Peptide accession
Q9UBL3
Residue number A
147
Residue number B
150
Peptide name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Ligandability
Cysteine 147 of Set1/Ash2 histone methyltransferase complex subunit ASH2
Cysteine 150 of Set1/Ash2 histone methyltransferase complex subunit ASH2
3rsn A 23 A 56
A redox-regulated disulphide may form within Set1/Ash2 histone methyltransferase complex subunit ASH2 between cysteines 117 and 150 (23 and 56 respectively in this structure).
Details
Redox score ?
83
PDB code
3rsn
Structure name
crystal structure of the n-terminal region of human ash2l
Structure deposition date
2011-05-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
10
Peptide accession
Q9UBL3
Residue number A
117
Residue number B
150
Peptide name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Ligandability
Cysteine 117 of Set1/Ash2 histone methyltransferase complex subunit ASH2
Cysteine 150 of Set1/Ash2 histone methyltransferase complex subunit ASH2
3s32 A 117 A 147
A redox-regulated disulphide may form within Set1/Ash2 histone methyltransferase complex subunit ASH2 between cysteines 117 and 147.
Details
Redox score ?
83
PDB code
3s32
Structure name
crystal structure of ash2l n-terminal domain
Structure deposition date
2011-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
9
Peptide accession
Q9UBL3
Residue number A
117
Residue number B
147
Peptide name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Ligandability
Cysteine 117 of Set1/Ash2 histone methyltransferase complex subunit ASH2
Cysteine 147 of Set1/Ash2 histone methyltransferase complex subunit ASH2
3rsn A 23 A 26
A redox-regulated disulphide may form within Set1/Ash2 histone methyltransferase complex subunit ASH2 between cysteines 117 and 120 (23 and 26 respectively in this structure).
Details
Redox score ?
83
PDB code
3rsn
Structure name
crystal structure of the n-terminal region of human ash2l
Structure deposition date
2011-05-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
13
Peptide accession
Q9UBL3
Residue number A
117
Residue number B
120
Peptide name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Ligandability
Cysteine 117 of Set1/Ash2 histone methyltransferase complex subunit ASH2
Cysteine 120 of Set1/Ash2 histone methyltransferase complex subunit ASH2
3s32 A 120 A 150
A redox-regulated disulphide may form within Set1/Ash2 histone methyltransferase complex subunit ASH2 between cysteines 120 and 150.
Details
Redox score ?
82
PDB code
3s32
Structure name
crystal structure of ash2l n-terminal domain
Structure deposition date
2011-05-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
2
Peptide accession
Q9UBL3
Residue number A
120
Residue number B
150
Peptide name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Ligandability
Cysteine 120 of Set1/Ash2 histone methyltransferase complex subunit ASH2
Cysteine 150 of Set1/Ash2 histone methyltransferase complex subunit ASH2
3s32 A 120 A 147
A redox-regulated disulphide may form within Set1/Ash2 histone methyltransferase complex subunit ASH2 between cysteines 120 and 147.
Details
Redox score ?
79
PDB code
3s32
Structure name
crystal structure of ash2l n-terminal domain
Structure deposition date
2011-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
3
Peptide accession
Q9UBL3
Residue number A
120
Residue number B
147
Peptide name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Ligandability
Cysteine 120 of Set1/Ash2 histone methyltransferase complex subunit ASH2
Cysteine 147 of Set1/Ash2 histone methyltransferase complex subunit ASH2
3rsn A 42 A 113
A redox-regulated disulphide may form within Set1/Ash2 histone methyltransferase complex subunit ASH2 between cysteines 136 and 207 (42 and 113 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
3rsn
Structure name
crystal structure of the n-terminal region of human ash2l
Structure deposition date
2011-05-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
44
Peptide accession
Q9UBL3
Residue number A
136
Residue number B
207
Peptide name
Set1/Ash2 histone methyltransferase complex subunit ASH2
Ligandability
Cysteine 136 of Set1/Ash2 histone methyltransferase complex subunit ASH2
Cysteine 207 of Set1/Ash2 histone methyltransferase complex subunit ASH2
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