ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DNA (cytosine-5)-methyltransferase 3A

Intermolecular
Cysteine 540 and cysteine 514
Cysteine 540 and cysteine 497
Intramolecular
Cysteine 494 and cysteine 514
Cysteine 494 and cysteine 497
Cysteine 494 and cysteine 517
Cysteine 549 and cysteine 586 L
Cysteine 514 and cysteine 517
Cysteine 549 and cysteine 554 L
Cysteine 549 and cysteine 583 L
Cysteine 540 and cysteine 559
More...
Cysteine 554 and cysteine 586 L
Cysteine 555 and cysteine 911 L
Cysteine 540 and cysteine 562 L
Cysteine 537 and cysteine 540
Cysteine 559 and cysteine 562 L
Cysteine 497 and cysteine 514
Cysteine 520 and cysteine 524
Cysteine 497 and cysteine 517
Cysteine 554 and cysteine 583 L
Cysteine 524 and cysteine 541
Cysteine 520 and cysteine 541
Cysteine 517 and cysteine 520
Cysteine 583 and cysteine 586
Cysteine 554 and cysteine 555 L
Cysteine 494 and cysteine 520
Cysteine 537 and cysteine 541
Cysteine 554 and cysteine 557 L
Cysteine 524 and cysteine 540
Cysteine 494 and cysteine 541
Cysteine 554 and cysteine 911 L
Cysteine 517 and cysteine 540
Cysteine 494 and cysteine 562 L
Cysteine 520 and cysteine 540
Cysteine 540 and cysteine 541
Cysteine 549 and cysteine 557 L
Cysteine 549 and cysteine 555 L
Cysteine 555 and cysteine 586 L
Cysteine 517 and cysteine 562 L
Cysteine 537 and cysteine 559
Cysteine 537 and cysteine 562 L
A redox-regulated disulphide may form between two units of DNA (cytosine-5)-methyltransferase 3A at cysteines 540 and 514. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
4qbq
Structure name
crystal structure of dnmt3a add domain bound to h3 peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
87
Minimum pKa ?
6
% buried
97
Peptide A name
DNA (cytosine-5)-methyltransferase 3A
Peptide B name
DNA (cytosine-5)-methyltransferase 3A
Peptide A accession
Q9Y6K1
Peptide B accession
Q9Y6K1
Peptide A residue number
540
Peptide B residue number
514

Ligandability

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 514 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of DNA (cytosine-5)-methyltransferase 3A at cysteines 540 and 497. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
4qbq
Structure name
crystal structure of dnmt3a add domain bound to h3 peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
6
% buried
nan
Peptide A name
DNA (cytosine-5)-methyltransferase 3A
Peptide B name
DNA (cytosine-5)-methyltransferase 3A
Peptide A accession
Q9Y6K1
Peptide B accession
Q9Y6K1
Peptide A residue number
540
Peptide B residue number
497

Ligandability

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 497 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 494 and 514.

Details

Redox score ?
86
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
3
% buried
37
Peptide accession
Q9Y6K1
Residue number A
494
Residue number B
514
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 494 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 514 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 494 and 497.

Details

Redox score ?
83
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
3
% buried
44
Peptide accession
Q9Y6K1
Residue number A
494
Residue number B
497
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 494 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 497 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 494 and 517.

Details

Redox score ?
83
PDB code
4u7p
Structure name
crystal structure of dnmt3a-dnmt3l complex
Structure deposition date
2014-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
48
Peptide accession
Q9Y6K1
Residue number A
494
Residue number B
517
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 494 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 517 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 549 and 586.

Details

Redox score ?
82
PDB code
3a1a
Structure name
crystal structure of the dnmt3a add domain
Structure deposition date
2009-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
23
Peptide accession
Q9Y6K1
Residue number A
549
Residue number B
586
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 549 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 586 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 514 and 517.

Details

Redox score ?
81
PDB code
4u7p
Structure name
crystal structure of dnmt3a-dnmt3l complex
Structure deposition date
2014-07-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
30
Peptide accession
Q9Y6K1
Residue number A
514
Residue number B
517
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 514 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 517 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 549 and 554.

Details

Redox score ?
81
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9Y6K1
Residue number A
549
Residue number B
554
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 549 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 554 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 549 and 583.

Details

Redox score ?
80
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
74
Minimum pKa ?
6
% buried
88
Peptide accession
Q9Y6K1
Residue number A
549
Residue number B
583
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 549 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 583 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 540 and 559.

Details

Redox score ?
79
PDB code
3a1b
Structure name
crystal structure of the dnmt3a add domain in complex with histone h3
Structure deposition date
2009-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
4
% buried
nan
Peptide accession
Q9Y6K1
Residue number A
540
Residue number B
559
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 559 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 554 and 586.

Details

Redox score ?
78
PDB code
4u7p
Structure name
crystal structure of dnmt3a-dnmt3l complex
Structure deposition date
2014-07-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
45
Minimum pKa ?
10
% buried
42
Peptide accession
Q9Y6K1
Residue number A
554
Residue number B
586
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 554 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 586 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 555 and 911.

Details

Redox score ?
78
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
80
Minimum pKa ?
6
% buried
82
Peptide accession
Q9Y6K1
Residue number A
555
Residue number B
911
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 555 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 911 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 540 and 562.

Details

Redox score ?
77
PDB code
4qbq
Structure name
crystal structure of dnmt3a add domain bound to h3 peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
4
% buried
98
Peptide accession
Q9Y6K1
Residue number A
540
Residue number B
562
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 562 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 537 and 540.

Details

Redox score ?
76
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
6
% buried
98
Peptide accession
Q9Y6K1
Residue number A
537
Residue number B
540
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 537 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 559 and 562.

Details

Redox score ?
75
PDB code
4qbs
Structure name
crystal structure of dnmt3a add domain e545r mutant bound to h3t3ph peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
6
% buried
82
Peptide accession
Q9Y6K1
Residue number A
559
Residue number B
562
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 559 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 562 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 497 and 514.

Details

Redox score ?
75
PDB code
4u7p
Structure name
crystal structure of dnmt3a-dnmt3l complex
Structure deposition date
2014-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
24
Peptide accession
Q9Y6K1
Residue number A
497
Residue number B
514
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 497 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 514 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 520 and 524.

Details

Redox score ?
73
PDB code
4qbs
Structure name
crystal structure of dnmt3a add domain e545r mutant bound to h3t3ph peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
22
Peptide accession
Q9Y6K1
Residue number A
520
Residue number B
524
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 520 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 524 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 497 and 517.

Details

Redox score ?
73
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
39
Peptide accession
Q9Y6K1
Residue number A
497
Residue number B
517
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 497 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 517 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 554 and 583.

Details

Redox score ?
71
PDB code
4u7p
Structure name
crystal structure of dnmt3a-dnmt3l complex
Structure deposition date
2014-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
60
Peptide accession
Q9Y6K1
Residue number A
554
Residue number B
583
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 554 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 583 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 524 and 541.

Details

Redox score ?
67
PDB code
4qbq
Structure name
crystal structure of dnmt3a add domain bound to h3 peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
90
Peptide accession
Q9Y6K1
Residue number A
524
Residue number B
541
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 524 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 541 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 520 and 541.

Details

Redox score ?
67
PDB code
4qbs
Structure name
crystal structure of dnmt3a add domain e545r mutant bound to h3t3ph peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
49
Peptide accession
Q9Y6K1
Residue number A
520
Residue number B
541
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 520 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 541 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 517 and 520.

Details

Redox score ?
66
PDB code
3a1a
Structure name
crystal structure of the dnmt3a add domain
Structure deposition date
2009-03-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
24
Peptide accession
Q9Y6K1
Residue number A
517
Residue number B
520
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 517 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 520 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 583 and 586.

Details

Redox score ?
63
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
15
% buried
84
Peptide accession
Q9Y6K1
Residue number A
583
Residue number B
586
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 583 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 586 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 554 and 555. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
4qbr
Structure name
crystal structure of dnmt3a add domain g550d mutant bound to h3 peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
30
Peptide accession
Q9Y6K1
Residue number A
554
Residue number B
555
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 554 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 555 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 494 and 520. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
8ba5
Structure name
crystal structure of the dnmt3a add domain
Structure deposition date
2022-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
3
% buried
35
Peptide accession
Q9Y6K1
Residue number A
494
Residue number B
520
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 494 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 520 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 537 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
4qbq
Structure name
crystal structure of dnmt3a add domain bound to h3 peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
5
% buried
nan
Peptide accession
Q9Y6K1
Residue number A
537
Residue number B
541
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 537 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 541 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 554 and 557. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
8ba5
Structure name
crystal structure of the dnmt3a add domain
Structure deposition date
2022-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
4
% buried
52
Peptide accession
Q9Y6K1
Residue number A
554
Residue number B
557
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 554 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 557 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 524 and 540. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3a1b
Structure name
crystal structure of the dnmt3a add domain in complex with histone h3
Structure deposition date
2009-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
4
% buried
72
Peptide accession
Q9Y6K1
Residue number A
524
Residue number B
540
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 524 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 494 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3a1b
Structure name
crystal structure of the dnmt3a add domain in complex with histone h3
Structure deposition date
2009-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
3
% buried
76
Peptide accession
Q9Y6K1
Residue number A
494
Residue number B
541
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 494 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 541 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 554 and 911. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9Y6K1
Residue number A
554
Residue number B
911
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 554 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 911 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 517 and 540. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3a1a
Structure name
crystal structure of the dnmt3a add domain
Structure deposition date
2009-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
6
% buried
53
Peptide accession
Q9Y6K1
Residue number A
517
Residue number B
540
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 517 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 494 and 562. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4qbs
Structure name
crystal structure of dnmt3a add domain e545r mutant bound to h3t3ph peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
2
% buried
74
Peptide accession
Q9Y6K1
Residue number A
494
Residue number B
562
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 494 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 562 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 520 and 540. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3a1b
Structure name
crystal structure of the dnmt3a add domain in complex with histone h3
Structure deposition date
2009-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
4
% buried
62
Peptide accession
Q9Y6K1
Residue number A
520
Residue number B
540
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 520 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 540 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4qbs
Structure name
crystal structure of dnmt3a add domain e545r mutant bound to h3t3ph peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
76
Peptide accession
Q9Y6K1
Residue number A
540
Residue number B
541
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 540 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 541 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 549 and 557. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
8ba5
Structure name
crystal structure of the dnmt3a add domain
Structure deposition date
2022-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
43
Peptide accession
Q9Y6K1
Residue number A
549
Residue number B
557
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 549 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 557 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 549 and 555. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4u7t
Structure name
crystal structure of dnmt3a-dnmt3l in complex with histone h3
Structure deposition date
2014-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
6
% buried
86
Peptide accession
Q9Y6K1
Residue number A
549
Residue number B
555
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 549 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 555 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 555 and 586. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4u7p
Structure name
crystal structure of dnmt3a-dnmt3l complex
Structure deposition date
2014-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
46
Peptide accession
Q9Y6K1
Residue number A
555
Residue number B
586
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 555 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 586 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 517 and 562. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4qbr
Structure name
crystal structure of dnmt3a add domain g550d mutant bound to h3 peptide
Structure deposition date
2014-05-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
6
% buried
70
Peptide accession
Q9Y6K1
Residue number A
517
Residue number B
562
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 517 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 562 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 537 and 559. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4u7p
Structure name
crystal structure of dnmt3a-dnmt3l complex
Structure deposition date
2014-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
22
% buried
nan
Peptide accession
Q9Y6K1
Residue number A
537
Residue number B
559
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 537 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 559 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within DNA (cytosine-5)-methyltransferase 3A between cysteines 537 and 562. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3a1a
Structure name
crystal structure of the dnmt3a add domain
Structure deposition date
2009-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
22
% buried
nan
Peptide accession
Q9Y6K1
Residue number A
537
Residue number B
562
Peptide name
DNA (cytosine-5)-methyltransferase 3A

Ligandability

Cysteine 537 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 562 of DNA (cytosine-5)-methyltransferase 3A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

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