N-lysine methyltransferase SMYD2
Intramolecular
Cysteine 209 and cysteine 267 L
Cysteine 55 and cysteine 74
Cysteine 262 and cysteine 267 L
Cysteine 55 and cysteine 78
Cysteine 68 and cysteine 90
Cysteine 65 and cysteine 90
Cysteine 264 and cysteine 267 L
Cysteine 65 and cysteine 68
Cysteine 52 and cysteine 74
Cysteine 209 and cysteine 264
More...Cysteine 74 and cysteine 78
Cysteine 52 and cysteine 54
Cysteine 52 and cysteine 78
Cysteine 262 and cysteine 264 L
Cysteine 210 and cysteine 264
Cysteine 52 and cysteine 55
Cysteine 54 and cysteine 78
Cysteine 209 and cysteine 262 L
Cysteine 210 and cysteine 262 L
Cysteine 41 and cysteine 52
Cysteine 209 and cysteine 210
Cysteine 54 and cysteine 74
Cysteine 54 and cysteine 55
Cysteine 41 and cysteine 54
Cysteine 321 and cysteine 350
Cysteine 210 and cysteine 267 L
Cysteine 41 and cysteine 78
Cysteine 41 and cysteine 55
5kjl A 209 A 267
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 209 and 267.
Details
Redox score ?
86
PDB code
5kjl
Structure name
smyd2 in complex with az378
Structure deposition date
2016-06-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
64
Peptide accession
Q9NRG4
Residue number A
209
Residue number B
267
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 209 of N-lysine methyltransferase SMYD2
Cysteine 267 of N-lysine methyltransferase SMYD2
3s7j A 55 A 74
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 55 and 74.
Details
Redox score ?
86
PDB code
3s7j
Structure name
structural basis of substrate methylation and inhibition of smyd2
Structure deposition date
2011-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
3
% buried
29
Peptide accession
Q9NRG4
Residue number A
55
Residue number B
74
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 55 of N-lysine methyltransferase SMYD2
Cysteine 74 of N-lysine methyltransferase SMYD2
5kjk A 262 A 267
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 262 and 267.
Details
Redox score ?
86
PDB code
5kjk
Structure name
smyd2 in complex with az370
Structure deposition date
2016-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
64
Peptide accession
Q9NRG4
Residue number A
262
Residue number B
267
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 262 of N-lysine methyltransferase SMYD2
Cysteine 267 of N-lysine methyltransferase SMYD2
6cby B 55 B 78
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 55 and 78.
Details
Redox score ?
85
PDB code
6cby
Structure name
crystal structure of human set and mynd domain containing protein 2 with mtf9975
Structure deposition date
2018-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
3
% buried
28
Peptide accession
Q9NRG4
Residue number A
55
Residue number B
78
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 55 of N-lysine methyltransferase SMYD2
Cysteine 78 of N-lysine methyltransferase SMYD2
5arf A 68 A 90
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 68 and 90.
Details
Redox score ?
84
PDB code
5arf
Structure name
smyd2 in complex with small molecule inhibitor compound-2
Structure deposition date
2015-09-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
42
Peptide accession
Q9NRG4
Residue number A
68
Residue number B
90
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 68 of N-lysine methyltransferase SMYD2
Cysteine 90 of N-lysine methyltransferase SMYD2
3s7d A 65 A 90
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 65 and 90.
Details
Redox score ?
83
PDB code
3s7d
Structure name
structural basis of substrate methylation and inhibition of smyd2
Structure deposition date
2011-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
32
Peptide accession
Q9NRG4
Residue number A
65
Residue number B
90
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 65 of N-lysine methyltransferase SMYD2
Cysteine 90 of N-lysine methyltransferase SMYD2
6n3g A 264 A 267
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 264 and 267.
Details
Redox score ?
82
PDB code
6n3g
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with polyethylene glycol
Structure deposition date
2018-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
nan
Peptide accession
Q9NRG4
Residue number A
264
Residue number B
267
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 264 of N-lysine methyltransferase SMYD2
Cysteine 267 of N-lysine methyltransferase SMYD2
6cbx A 65 A 68
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 65 and 68.
Details
Redox score ?
81
PDB code
6cbx
Structure name
crystal structure of human set and mynd domain containing protein 2 with mtf1497
Structure deposition date
2018-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NRG4
Residue number A
65
Residue number B
68
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 65 of N-lysine methyltransferase SMYD2
Cysteine 68 of N-lysine methyltransferase SMYD2
5arf A 52 A 74
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 52 and 74.
Details
Redox score ?
75
PDB code
5arf
Structure name
smyd2 in complex with small molecule inhibitor compound-2
Structure deposition date
2015-09-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
31
Peptide accession
Q9NRG4
Residue number A
52
Residue number B
74
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 52 of N-lysine methyltransferase SMYD2
Cysteine 74 of N-lysine methyltransferase SMYD2
6cbx A 209 A 264
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 209 and 264.
Details
Redox score ?
75
PDB code
6cbx
Structure name
crystal structure of human set and mynd domain containing protein 2 with mtf1497
Structure deposition date
2018-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NRG4
Residue number A
209
Residue number B
264
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 209 of N-lysine methyltransferase SMYD2
Cysteine 264 of N-lysine methyltransferase SMYD2
6cby A 74 A 78
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 74 and 78.
Details
Redox score ?
74
PDB code
6cby
Structure name
crystal structure of human set and mynd domain containing protein 2 with mtf9975
Structure deposition date
2018-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
14
Peptide accession
Q9NRG4
Residue number A
74
Residue number B
78
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 74 of N-lysine methyltransferase SMYD2
Cysteine 78 of N-lysine methyltransferase SMYD2
3qwv A 52 A 54
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 52 and 54.
Details
Redox score ?
73
PDB code
3qwv
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the cofactor product adohcy
Structure deposition date
2011-02-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
3
% buried
55
Peptide accession
Q8R5A0
Residue number A
52
Residue number B
54
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 52 of N-lysine methyltransferase SMYD2
Cysteine 54 of N-lysine methyltransferase SMYD2
6cbx A 52 A 78
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 52 and 78.
Details
Redox score ?
73
PDB code
6cbx
Structure name
crystal structure of human set and mynd domain containing protein 2 with mtf1497
Structure deposition date
2018-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NRG4
Residue number A
52
Residue number B
78
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 52 of N-lysine methyltransferase SMYD2
Cysteine 78 of N-lysine methyltransferase SMYD2
6mon A 262 A 264
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 262 and 264.
Details
Redox score ?
69
PDB code
6mon
Structure name
crystal structure of human smyd2 in complex with nle-peptide inhibitor
Structure deposition date
2018-10-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
14
% buried
nan
Peptide accession
Q9NRG4
Residue number A
262
Residue number B
264
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 262 of N-lysine methyltransferase SMYD2
Cysteine 264 of N-lysine methyltransferase SMYD2
6cbx A 210 A 264
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 210 and 264.
Details
Redox score ?
69
PDB code
6cbx
Structure name
crystal structure of human set and mynd domain containing protein 2 with mtf1497
Structure deposition date
2018-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NRG4
Residue number A
210
Residue number B
264
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 210 of N-lysine methyltransferase SMYD2
Cysteine 264 of N-lysine methyltransferase SMYD2
6cbx A 52 A 55
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 52 and 55.
Details
Redox score ?
68
PDB code
6cbx
Structure name
crystal structure of human set and mynd domain containing protein 2 with mtf1497
Structure deposition date
2018-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NRG4
Residue number A
52
Residue number B
55
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 52 of N-lysine methyltransferase SMYD2
Cysteine 55 of N-lysine methyltransferase SMYD2
3qwv A 54 A 78
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 54 and 78.
Details
Redox score ?
66
PDB code
3qwv
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the cofactor product adohcy
Structure deposition date
2011-02-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
40
Peptide accession
Q8R5A0
Residue number A
54
Residue number B
78
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 54 of N-lysine methyltransferase SMYD2
Cysteine 78 of N-lysine methyltransferase SMYD2
3s7d A 209 A 262
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 209 and 262.
Details
Redox score ?
62
PDB code
3s7d
Structure name
structural basis of substrate methylation and inhibition of smyd2
Structure deposition date
2011-05-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
14
% buried
80
Peptide accession
Q9NRG4
Residue number A
209
Residue number B
262
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 209 of N-lysine methyltransferase SMYD2
Cysteine 262 of N-lysine methyltransferase SMYD2
5wcg A 210 A 262
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 210 and 262. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5wcg
Structure name
set and mynd domain containing protein 2
Structure deposition date
2017-06-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NRG4
Residue number A
210
Residue number B
262
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 210 of N-lysine methyltransferase SMYD2
Cysteine 262 of N-lysine methyltransferase SMYD2
3qww A 41 A 52
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 41 and 52. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3qww
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the methyltransferase inhibitor sinefungin
Structure deposition date
2011-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
3
% buried
78
Peptide accession
Q8R5A0
Residue number A
41
Residue number B
52
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 41 of N-lysine methyltransferase SMYD2
Cysteine 52 of N-lysine methyltransferase SMYD2
3qww A 209 A 210
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 209 and 210. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3qww
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the methyltransferase inhibitor sinefungin
Structure deposition date
2011-02-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
60
Peptide accession
Q8R5A0
Residue number A
209
Residue number B
210
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 209 of N-lysine methyltransferase SMYD2
Cysteine 210 of N-lysine methyltransferase SMYD2
3qww A 54 A 74
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 54 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3qww
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the methyltransferase inhibitor sinefungin
Structure deposition date
2011-02-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
40
Peptide accession
Q8R5A0
Residue number A
54
Residue number B
74
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 54 of N-lysine methyltransferase SMYD2
Cysteine 74 of N-lysine methyltransferase SMYD2
3qwv A 54 A 55
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 54 and 55. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3qwv
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the cofactor product adohcy
Structure deposition date
2011-02-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
55
Peptide accession
Q8R5A0
Residue number A
54
Residue number B
55
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 54 of N-lysine methyltransferase SMYD2
Cysteine 55 of N-lysine methyltransferase SMYD2
3qww A 41 A 54
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 41 and 54. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3qww
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the methyltransferase inhibitor sinefungin
Structure deposition date
2011-02-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
80
Peptide accession
Q8R5A0
Residue number A
41
Residue number B
54
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 41 of N-lysine methyltransferase SMYD2
Cysteine 54 of N-lysine methyltransferase SMYD2
3qww A 321 A 350
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 321 and 350. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3qww
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the methyltransferase inhibitor sinefungin
Structure deposition date
2011-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
56
Peptide accession
Q8R5A0
Residue number A
321
Residue number B
350
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 321 of N-lysine methyltransferase SMYD2
Cysteine 350 of N-lysine methyltransferase SMYD2
5arg A 210 A 267
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 210 and 267. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5arg
Structure name
smyd2 in complex with sgc probe bay-598
Structure deposition date
2015-09-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9NRG4
Residue number A
210
Residue number B
267
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 210 of N-lysine methyltransferase SMYD2
Cysteine 267 of N-lysine methyltransferase SMYD2
3qww A 41 A 78
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 41 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3qww
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the methyltransferase inhibitor sinefungin
Structure deposition date
2011-02-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
64
Peptide accession
Q8R5A0
Residue number A
41
Residue number B
78
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 41 of N-lysine methyltransferase SMYD2
Cysteine 78 of N-lysine methyltransferase SMYD2
3qww A 41 A 55
A redox-regulated disulphide may form within N-lysine methyltransferase SMYD2 between cysteines 41 and 55. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3qww
Structure name
crystal structure of histone lysine methyltransferase smyd2 in complex with the methyltransferase inhibitor sinefungin
Structure deposition date
2011-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
78
Peptide accession
Q8R5A0
Residue number A
41
Residue number B
55
Peptide name
N-lysine methyltransferase SMYD2
Ligandability
Cysteine 41 of N-lysine methyltransferase SMYD2
Cysteine 55 of N-lysine methyltransferase SMYD2
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