Histone-arginine methyltransferase CARM1
Intramolecular
Cysteine 91 and cysteine 128
Cysteine 420 and cysteine 438
Cysteine 79 and cysteine 83
Cysteine 83 and cysteine 128
Cysteine 83 and cysteine 91
2oqb B 91 B 128
A redox-regulated disulphide may form within Histone-arginine methyltransferase CARM1 between cysteines 91 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2oqb
Structure name
crystal structure of the n-terminal domain of coactivator-associated methyltransferase 1 (carm1)
Structure deposition date
2007-01-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
56
Peptide accession
Q4AE70
Residue number A
91
Residue number B
128
Peptide name
Histone-arginine methyltransferase CARM1
Ligandability
Cysteine 91 of Histone-arginine methyltransferase CARM1
Cysteine 128 of Histone-arginine methyltransferase CARM1
5dx8 C 420 C 438
A redox-regulated disulphide may form within Histone-arginine methyltransferase CARM1 between cysteines 420 and 438. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5dx8
Structure name
crystal structure of carm1, sinefungin, and methylated pabp1 peptide (r455)
Structure deposition date
2015-09-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
Q86X55
Residue number A
420
Residue number B
438
Peptide name
Histone-arginine methyltransferase CARM1
Ligandability
Cysteine 420 of Histone-arginine methyltransferase CARM1
Cysteine 438 of Histone-arginine methyltransferase CARM1
2oqb B 79 B 83
A redox-regulated disulphide may form within Histone-arginine methyltransferase CARM1 between cysteines 79 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2oqb
Structure name
crystal structure of the n-terminal domain of coactivator-associated methyltransferase 1 (carm1)
Structure deposition date
2007-01-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
36
Peptide accession
Q4AE70
Residue number A
79
Residue number B
83
Peptide name
Histone-arginine methyltransferase CARM1
Ligandability
Cysteine 79 of Histone-arginine methyltransferase CARM1
Cysteine 83 of Histone-arginine methyltransferase CARM1
2oqb B 83 B 128
A redox-regulated disulphide may form within Histone-arginine methyltransferase CARM1 between cysteines 83 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2oqb
Structure name
crystal structure of the n-terminal domain of coactivator-associated methyltransferase 1 (carm1)
Structure deposition date
2007-01-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
10
% buried
48
Peptide accession
Q4AE70
Residue number A
83
Residue number B
128
Peptide name
Histone-arginine methyltransferase CARM1
Ligandability
Cysteine 83 of Histone-arginine methyltransferase CARM1
Cysteine 128 of Histone-arginine methyltransferase CARM1
2oqb A 83 A 91
A redox-regulated disulphide may form within Histone-arginine methyltransferase CARM1 between cysteines 83 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2oqb
Structure name
crystal structure of the n-terminal domain of coactivator-associated methyltransferase 1 (carm1)
Structure deposition date
2007-01-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
76
Peptide accession
Q4AE70
Residue number A
83
Residue number B
91
Peptide name
Histone-arginine methyltransferase CARM1
Ligandability
Cysteine 83 of Histone-arginine methyltransferase CARM1
Cysteine 91 of Histone-arginine methyltransferase CARM1
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