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Histone-lysine N-methyltransferase EZH1

Intramolecular
Cysteine 589 and cysteine 602
Cysteine 524 and cysteine 548
Cysteine 561 and cysteine 589
Cysteine 537 and cysteine 548
Cysteine 531 and cysteine 535
Cysteine 544 and cysteine 548
Cysteine 581 and cysteine 589
Cysteine 550 and cysteine 554
Cysteine 561 and cysteine 586
Cysteine 524 and cysteine 550
More...
Cysteine 574 and cysteine 586
Cysteine 563 and cysteine 572
Cysteine 524 and cysteine 535
Cysteine 567 and cysteine 572
Cysteine 535 and cysteine 537
Cysteine 531 and cysteine 554
Cysteine 561 and cysteine 572
Cysteine 535 and cysteine 544
Cysteine 544 and cysteine 554
Cysteine 572 and cysteine 574
Cysteine 524 and cysteine 531
Cysteine 302 and cysteine 307
Cysteine 561 and cysteine 563
Cysteine 531 and cysteine 544
Cysteine 586 and cysteine 589
Cysteine 524 and cysteine 544
Cysteine 333 and cysteine 454
Cysteine 333 and cysteine 337
Cysteine 337 and cysteine 454
Cysteine 299 and cysteine 302
Cysteine 572 and cysteine 581
Cysteine 561 and cysteine 574
Cysteine 563 and cysteine 567
Cysteine 299 and cysteine 307
Cysteine 454 and cysteine 465
Cysteine 544 and cysteine 550
Cysteine 524 and cysteine 537
Cysteine 561 and cysteine 581
Cysteine 531 and cysteine 550
Cysteine 337 and cysteine 465
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EZH1 between cysteines 589 and 602.

Details

Redox score ?
96
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
0
% buried
60
Peptide accession
Q92800
Residue number A
589
Residue number B
602
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 589 of Histone-lysine N-methyltransferase EZH1

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 602 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 524 and 548.

Details

Redox score ?
94
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
2
% buried
40
Peptide accession
Q92800
Residue number A
524
Residue number B
548
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 524 of Histone-lysine N-methyltransferase EZH1

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 548 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 561 and 589.

Details

Redox score ?
93
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
0
% buried
44
Peptide accession
Q92800
Residue number A
561
Residue number B
589
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 561 of Histone-lysine N-methyltransferase EZH1

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 589 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 537 and 548.

Details

Redox score ?
92
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
2
% buried
52
Peptide accession
Q92800
Residue number A
537
Residue number B
548
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 537 of Histone-lysine N-methyltransferase EZH1

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 548 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 531 and 535.

Details

Redox score ?
92
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
4
% buried
19
Peptide accession
Q92800
Residue number A
531
Residue number B
535
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 531 of Histone-lysine N-methyltransferase EZH1

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 535 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 544 and 548.

Details

Redox score ?
91
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
2
% buried
45
Peptide accession
Q92800
Residue number A
544
Residue number B
548
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 544 of Histone-lysine N-methyltransferase EZH1

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 548 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 581 and 589.

Details

Redox score ?
91
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
0
% buried
nan
Peptide accession
Q92800
Residue number A
581
Residue number B
589
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 581 of Histone-lysine N-methyltransferase EZH1

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 589 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 550 and 554.

Details

Redox score ?
90
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
18
Peptide accession
Q92800
Residue number A
550
Residue number B
554
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 550 of Histone-lysine N-methyltransferase EZH1

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 554 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 561 and 586.

Details

Redox score ?
88
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
4
% buried
56
Peptide accession
Q92800
Residue number A
561
Residue number B
586
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 561 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 524 and 550.

Details

Redox score ?
88
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
25
Peptide accession
Q92800
Residue number A
524
Residue number B
550
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 524 of Histone-lysine N-methyltransferase EZH1

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 550 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 574 and 586.

Details

Redox score ?
88
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
4
% buried
64
Peptide accession
Q92800
Residue number A
574
Residue number B
586
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 574 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 563 and 572.

Details

Redox score ?
87
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
24
Peptide accession
Q92800
Residue number A
563
Residue number B
572
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 563 of Histone-lysine N-methyltransferase EZH1

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 572 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 524 and 535.

Details

Redox score ?
86
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
4
% buried
33
Peptide accession
Q92800
Residue number A
524
Residue number B
535
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 524 of Histone-lysine N-methyltransferase EZH1

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 535 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 567 and 572.

Details

Redox score ?
86
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
40
Peptide accession
Q92800
Residue number A
567
Residue number B
572
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 567 of Histone-lysine N-methyltransferase EZH1

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 572 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 535 and 537.

Details

Redox score ?
86
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
4
% buried
41
Peptide accession
Q92800
Residue number A
535
Residue number B
537
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 535 of Histone-lysine N-methyltransferase EZH1

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 537 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 531 and 554.

Details

Redox score ?
86
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
10
Peptide accession
Q92800
Residue number A
531
Residue number B
554
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 531 of Histone-lysine N-methyltransferase EZH1

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 554 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 561 and 572.

Details

Redox score ?
84
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
38
Peptide accession
Q92800
Residue number A
561
Residue number B
572
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 561 of Histone-lysine N-methyltransferase EZH1

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 572 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 535 and 544.

Details

Redox score ?
84
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
4
% buried
32
Peptide accession
Q92800
Residue number A
535
Residue number B
544
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 535 of Histone-lysine N-methyltransferase EZH1

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 544 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 544 and 554.

Details

Redox score ?
83
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
28
Peptide accession
Q92800
Residue number A
544
Residue number B
554
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 544 of Histone-lysine N-methyltransferase EZH1

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 554 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 572 and 574.

Details

Redox score ?
82
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
47
Peptide accession
Q92800
Residue number A
572
Residue number B
574
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 572 of Histone-lysine N-methyltransferase EZH1

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 574 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 524 and 531.

Details

Redox score ?
82
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
18
Peptide accession
Q92800
Residue number A
524
Residue number B
531
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 524 of Histone-lysine N-methyltransferase EZH1

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 531 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 302 and 307.

Details

Redox score ?
81
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
5
% buried
98
Peptide accession
Q92800
Residue number A
302
Residue number B
307
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 302 of Histone-lysine N-methyltransferase EZH1

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 307 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 561 and 563.

Details

Redox score ?
80
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
26
Peptide accession
Q92800
Residue number A
561
Residue number B
563
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 561 of Histone-lysine N-methyltransferase EZH1

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 563 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 531 and 544.

Details

Redox score ?
80
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
30
Peptide accession
Q92800
Residue number A
531
Residue number B
544
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 531 of Histone-lysine N-methyltransferase EZH1

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 544 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 586 and 589.

Details

Redox score ?
80
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
4
% buried
58
Peptide accession
Q92800
Residue number A
586
Residue number B
589
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 586 of Histone-lysine N-methyltransferase EZH1

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 589 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 524 and 544.

Details

Redox score ?
80
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
44
Peptide accession
Q92800
Residue number A
524
Residue number B
544
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 524 of Histone-lysine N-methyltransferase EZH1

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 544 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 333 and 454.

Details

Redox score ?
79
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
32
Peptide accession
Q92800
Residue number A
333
Residue number B
454
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 333 of Histone-lysine N-methyltransferase EZH1

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 454 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 333 and 337.

Details

Redox score ?
79
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
21
Peptide accession
Q92800
Residue number A
333
Residue number B
337
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 333 of Histone-lysine N-methyltransferase EZH1

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 337 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 337 and 454.

Details

Redox score ?
79
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
5
% buried
36
Peptide accession
Q92800
Residue number A
337
Residue number B
454
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 337 of Histone-lysine N-methyltransferase EZH1

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 454 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 299 and 302.

Details

Redox score ?
79
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
nan
Peptide accession
Q92800
Residue number A
299
Residue number B
302
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 299 of Histone-lysine N-methyltransferase EZH1

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 302 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 572 and 581.

Details

Redox score ?
79
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
6
% buried
nan
Peptide accession
Q92800
Residue number A
572
Residue number B
581
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 572 of Histone-lysine N-methyltransferase EZH1

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 581 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 561 and 574.

Details

Redox score ?
78
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
50
Peptide accession
Q92800
Residue number A
561
Residue number B
574
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 561 of Histone-lysine N-methyltransferase EZH1

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 574 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 563 and 567.

Details

Redox score ?
78
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
27
Peptide accession
Q92800
Residue number A
563
Residue number B
567
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 563 of Histone-lysine N-methyltransferase EZH1

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 567 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 299 and 307.

Details

Redox score ?
78
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
84
Peptide accession
Q92800
Residue number A
299
Residue number B
307
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 299 of Histone-lysine N-methyltransferase EZH1

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 307 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 454 and 465.

Details

Redox score ?
78
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
5
% buried
54
Peptide accession
Q92800
Residue number A
454
Residue number B
465
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 454 of Histone-lysine N-methyltransferase EZH1

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 465 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 544 and 550.

Details

Redox score ?
78
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
42
Peptide accession
Q92800
Residue number A
544
Residue number B
550
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 544 of Histone-lysine N-methyltransferase EZH1

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 550 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 524 and 537.

Details

Redox score ?
77
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
36
Peptide accession
Q92800
Residue number A
524
Residue number B
537
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 524 of Histone-lysine N-methyltransferase EZH1

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 537 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 561 and 581.

Details

Redox score ?
76
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
nan
Peptide accession
Q92800
Residue number A
561
Residue number B
581
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 561 of Histone-lysine N-methyltransferase EZH1

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 581 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 531 and 550.

Details

Redox score ?
76
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
30
Peptide accession
Q92800
Residue number A
531
Residue number B
550
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 531 of Histone-lysine N-methyltransferase EZH1

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 550 of Histone-lysine N-methyltransferase EZH1

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 Histone-lysine N-methyltransferase EZH1 between cysteines 337 and 465.

Details

Redox score ?
76
PDB code
7td5
Structure name
structure of human prc2-ezh1 containing phosphorylated suz12
Structure deposition date
2021-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
43
Peptide accession
Q92800
Residue number A
337
Residue number B
465
Peptide name
Histone-lysine N-methyltransferase EZH1

Ligandability

Cysteine 337 of Histone-lysine N-methyltransferase EZH1

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 465 of Histone-lysine N-methyltransferase EZH1

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.

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