Histone-lysine N-methyltransferase SMYD3
Intramolecular
Cysteine 62 and cysteine 65
Cysteine 62 and cysteine 87
Cysteine 261 and cysteine 266
Cysteine 65 and cysteine 87
Cysteine 49 and cysteine 75
Cysteine 49 and cysteine 71
Cysteine 208 and cysteine 266
Cysteine 49 and cysteine 52
Cysteine 263 and cysteine 266 L
Cysteine 261 and cysteine 263 L
More...Cysteine 71 and cysteine 75
Cysteine 52 and cysteine 71
Cysteine 52 and cysteine 75
Cysteine 208 and cysteine 261
Cysteine 208 and cysteine 238
Cysteine 309 and cysteine 333
Cysteine 238 and cysteine 263 L
Cysteine 238 and cysteine 266
Cysteine 180 and cysteine 258 L
Cysteine 65 and cysteine 93
Cysteine 208 and cysteine 263 L
Cysteine 65 and cysteine 89
Cysteine 89 and cysteine 93
Cysteine 238 and cysteine 261
Cysteine 309 and cysteine 338
Cysteine 87 and cysteine 89
Cysteine 41 and cysteine 186
7o2b A 62 A 65
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 62 and 65.
Details
Redox score ?
92
PDB code
7o2b
Structure name
x-ray structure of smyd3 in complex with benzodiazepine-type inhibitor 6
Structure deposition date
2021-03-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
4
% buried
40
Peptide accession
Q9H7B4
Residue number A
62
Residue number B
65
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 62 of Histone-lysine N-methyltransferase SMYD3
Cysteine 65 of Histone-lysine N-methyltransferase SMYD3
5hq8 B 62 B 87
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 62 and 87.
Details
Redox score ?
91
PDB code
5hq8
Structure name
co-crystal structure of human smyd3 with a mekk2 peptide at 2
Structure deposition date
2016-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
1
% buried
55
Peptide accession
Q9H7B4
Residue number A
62
Residue number B
87
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 62 of Histone-lysine N-methyltransferase SMYD3
Cysteine 87 of Histone-lysine N-methyltransferase SMYD3
3oxf B 261 B 266
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 261 and 266.
Details
Redox score ?
89
PDB code
3oxf
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form i)
Structure deposition date
2010-09-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
53
Peptide accession
Q9H7B4
Residue number A
261
Residue number B
266
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 261 of Histone-lysine N-methyltransferase SMYD3
Cysteine 266 of Histone-lysine N-methyltransferase SMYD3
3oxf A 65 A 87
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 65 and 87.
Details
Redox score ?
88
PDB code
3oxf
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form i)
Structure deposition date
2010-09-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
46
Peptide accession
Q9H7B4
Residue number A
65
Residue number B
87
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 65 of Histone-lysine N-methyltransferase SMYD3
Cysteine 87 of Histone-lysine N-methyltransferase SMYD3
6ijl A 49 A 75
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 49 and 75.
Details
Redox score ?
87
PDB code
6ijl
Structure name
crystal structure of smyd3 in complex with covalent inhibitor 5
Structure deposition date
2018-10-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
4
% buried
35
Peptide accession
Q9H7B4
Residue number A
49
Residue number B
75
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 49 of Histone-lysine N-methyltransferase SMYD3
Cysteine 75 of Histone-lysine N-methyltransferase SMYD3
7o2b A 49 A 71
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 49 and 71.
Details
Redox score ?
87
PDB code
7o2b
Structure name
x-ray structure of smyd3 in complex with benzodiazepine-type inhibitor 6
Structure deposition date
2021-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
3
% buried
24
Peptide accession
Q9H7B4
Residue number A
49
Residue number B
71
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 49 of Histone-lysine N-methyltransferase SMYD3
Cysteine 71 of Histone-lysine N-methyltransferase SMYD3
5ccl A 208 A 266
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 208 and 266.
Details
Redox score ?
86
PDB code
5ccl
Structure name
crystal structure of smyd3 with sam and oxindole compound
Structure deposition date
2015-07-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
5
% buried
64
Peptide accession
Q9H7B4
Residue number A
208
Residue number B
266
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 208 of Histone-lysine N-methyltransferase SMYD3
Cysteine 266 of Histone-lysine N-methyltransferase SMYD3
3oxl A 49 A 52
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 49 and 52.
Details
Redox score ?
83
PDB code
3oxl
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form ii)
Structure deposition date
2010-09-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
3
% buried
49
Peptide accession
Q9H7B4
Residue number A
49
Residue number B
52
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 49 of Histone-lysine N-methyltransferase SMYD3
Cysteine 52 of Histone-lysine N-methyltransferase SMYD3
5ex3 A 263 A 266
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 263 and 266.
Details
Redox score ?
83
PDB code
5ex3
Structure name
crystal structure of human smyd3 in complex with a vegfr1 peptide
Structure deposition date
2015-11-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
nan
Peptide accession
Q9H7B4
Residue number A
263
Residue number B
266
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 263 of Histone-lysine N-methyltransferase SMYD3
Cysteine 266 of Histone-lysine N-methyltransferase SMYD3
3oxf A 261 A 263
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 261 and 263.
Details
Redox score ?
81
PDB code
3oxf
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form i)
Structure deposition date
2010-09-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
5
% buried
88
Peptide accession
Q9H7B4
Residue number A
261
Residue number B
263
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 261 of Histone-lysine N-methyltransferase SMYD3
Cysteine 263 of Histone-lysine N-methyltransferase SMYD3
7o2a A 71 A 75
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 71 and 75.
Details
Redox score ?
80
PDB code
7o2a
Structure name
x-ray structure of smyd3 in complex with benzodiazepine-type inhibitor compound 15
Structure deposition date
2021-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
14
Peptide accession
Q9H7B4
Residue number A
71
Residue number B
75
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 71 of Histone-lysine N-methyltransferase SMYD3
Cysteine 75 of Histone-lysine N-methyltransferase SMYD3
3oxl A 52 A 71
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 52 and 71.
Details
Redox score ?
76
PDB code
3oxl
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form ii)
Structure deposition date
2010-09-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
26
Peptide accession
Q9H7B4
Residue number A
52
Residue number B
71
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 52 of Histone-lysine N-methyltransferase SMYD3
Cysteine 71 of Histone-lysine N-methyltransferase SMYD3
5ccm A 52 A 75
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 52 and 75.
Details
Redox score ?
72
PDB code
5ccm
Structure name
crystal structure of smyd3 with sam and epz030456
Structure deposition date
2015-07-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
37
Peptide accession
Q9H7B4
Residue number A
52
Residue number B
75
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 52 of Histone-lysine N-methyltransferase SMYD3
Cysteine 75 of Histone-lysine N-methyltransferase SMYD3
3oxl A 208 A 261
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 208 and 261.
Details
Redox score ?
69
PDB code
3oxl
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form ii)
Structure deposition date
2010-09-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
14
% buried
68
Peptide accession
Q9H7B4
Residue number A
208
Residue number B
261
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 208 of Histone-lysine N-methyltransferase SMYD3
Cysteine 261 of Histone-lysine N-methyltransferase SMYD3
3mek A 208 A 238
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 208 and 238. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
3mek
Structure name
crystal structure of human histone-lysine n-methyltransferase smyd3 in complex with s-adenosyl-l-methionine
Structure deposition date
2010-03-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
85
Peptide accession
Q9H7B4
Residue number A
208
Residue number B
238
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 208 of Histone-lysine N-methyltransferase SMYD3
Cysteine 238 of Histone-lysine N-methyltransferase SMYD3
3mek A 309 A 333
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 309 and 333. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
3mek
Structure name
crystal structure of human histone-lysine n-methyltransferase smyd3 in complex with s-adenosyl-l-methionine
Structure deposition date
2010-03-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
90
Peptide accession
Q9H7B4
Residue number A
309
Residue number B
333
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 309 of Histone-lysine N-methyltransferase SMYD3
Cysteine 333 of Histone-lysine N-methyltransferase SMYD3
7qa6 A 238 A 263
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 238 and 263. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
7qa6
Structure name
smyd3 in complex with fragment fl01507
Structure deposition date
2021-11-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
4
% buried
74
Peptide accession
Q9H7B4
Residue number A
238
Residue number B
263
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 238 of Histone-lysine N-methyltransferase SMYD3
Cysteine 263 of Histone-lysine N-methyltransferase SMYD3
5hq8 B 238 B 266
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 238 and 266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5hq8
Structure name
co-crystal structure of human smyd3 with a mekk2 peptide at 2
Structure deposition date
2016-01-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
74
Peptide accession
Q9H7B4
Residue number A
238
Residue number B
266
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 238 of Histone-lysine N-methyltransferase SMYD3
Cysteine 266 of Histone-lysine N-methyltransferase SMYD3
3oxl A 180 A 258
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 180 and 258. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
3oxl
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form ii)
Structure deposition date
2010-09-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
66
Peptide accession
Q9H7B4
Residue number A
180
Residue number B
258
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 180 of Histone-lysine N-methyltransferase SMYD3
Cysteine 258 of Histone-lysine N-methyltransferase SMYD3
5hq8 A 65 A 93
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 65 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5hq8
Structure name
co-crystal structure of human smyd3 with a mekk2 peptide at 2
Structure deposition date
2016-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
45
Minimum pKa ?
5
% buried
45
Peptide accession
Q9H7B4
Residue number A
65
Residue number B
93
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 65 of Histone-lysine N-methyltransferase SMYD3
Cysteine 93 of Histone-lysine N-methyltransferase SMYD3
6paf A 208 A 263
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 208 and 263. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6paf
Structure name
co-crystal structure of human smyd3 with isoxazole amides inhibitors
Structure deposition date
2019-06-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
23
% buried
nan
Peptide accession
Q9H7B4
Residue number A
208
Residue number B
263
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 208 of Histone-lysine N-methyltransferase SMYD3
Cysteine 263 of Histone-lysine N-methyltransferase SMYD3
3oxf B 65 B 89
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 65 and 89. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3oxf
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form i)
Structure deposition date
2010-09-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
64
Peptide accession
Q9H7B4
Residue number A
65
Residue number B
89
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 65 of Histone-lysine N-methyltransferase SMYD3
Cysteine 89 of Histone-lysine N-methyltransferase SMYD3
5ccm A 89 A 93
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 89 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5ccm
Structure name
crystal structure of smyd3 with sam and epz030456
Structure deposition date
2015-07-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
50
Peptide accession
Q9H7B4
Residue number A
89
Residue number B
93
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 89 of Histone-lysine N-methyltransferase SMYD3
Cysteine 93 of Histone-lysine N-methyltransferase SMYD3
7qa6 A 238 A 261
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 238 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7qa6
Structure name
smyd3 in complex with fragment fl01507
Structure deposition date
2021-11-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
78
Peptide accession
Q9H7B4
Residue number A
238
Residue number B
261
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 238 of Histone-lysine N-methyltransferase SMYD3
Cysteine 261 of Histone-lysine N-methyltransferase SMYD3
5hq8 B 309 B 338
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 309 and 338. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5hq8
Structure name
co-crystal structure of human smyd3 with a mekk2 peptide at 2
Structure deposition date
2016-01-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
64
Peptide accession
Q9H7B4
Residue number A
309
Residue number B
338
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 309 of Histone-lysine N-methyltransferase SMYD3
Cysteine 338 of Histone-lysine N-methyltransferase SMYD3
3oxf A 87 A 89
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 87 and 89. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3oxf
Structure name
human lysine methyltransferase smyd3 in complex with adohcy (form i)
Structure deposition date
2010-09-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
52
Peptide accession
Q9H7B4
Residue number A
87
Residue number B
89
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 87 of Histone-lysine N-methyltransferase SMYD3
Cysteine 89 of Histone-lysine N-methyltransferase SMYD3
5ccl A 41 A 186
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase SMYD3 between cysteines 41 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
5ccl
Structure name
crystal structure of smyd3 with sam and oxindole compound
Structure deposition date
2015-07-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
88
Peptide accession
Q9H7B4
Residue number A
41
Residue number B
186
Peptide name
Histone-lysine N-methyltransferase SMYD3
Ligandability
Cysteine 41 of Histone-lysine N-methyltransferase SMYD3
Cysteine 186 of Histone-lysine N-methyltransferase SMYD3
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