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Histone-lysine N-methyltransferase EZH2

Intramolecular
Cysteine 530 and cysteine 534
Cysteine 562 and cysteine 571
Cysteine 562 and cysteine 566
Cysteine 324 and cysteine 463
Cysteine 560 and cysteine 571
Cysteine 536 and cysteine 547
Cysteine 523 and cysteine 534
Cysteine 530 and cysteine 549
Cysteine 560 and cysteine 562
Cysteine 320 and cysteine 452
More...
Cysteine 566 and cysteine 571
Cysteine 534 and cysteine 536
Cysteine 534 and cysteine 543
Cysteine 566 and cysteine 588
Cysteine 560 and cysteine 588
Cysteine 571 and cysteine 580
Cysteine 452 and cysteine 463
Cysteine 530 and cysteine 553
Cysteine 580 and cysteine 588
Cysteine 286 and cysteine 289
Cysteine 548 and cysteine 552
Cysteine 566 and cysteine 585
Cysteine 560 and cysteine 585
Cysteine 286 and cysteine 294
Cysteine 549 and cysteine 553
Cysteine 548 and cysteine 558
Cysteine 560 and cysteine 566
Cysteine 528 and cysteine 535
Cysteine 320 and cysteine 324
Cysteine 552 and cysteine 554
Cysteine 580 and cysteine 585
Cysteine 523 and cysteine 543
Cysteine 571 and cysteine 573
Cysteine 547 and cysteine 553
Cysteine 573 and cysteine 580
Cysteine 566 and cysteine 601
Cysteine 523 and cysteine 536
Cysteine 523 and cysteine 549
Cysteine 588 and cysteine 601
Cysteine 548 and cysteine 554
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase EZH2 between cysteines 530 and 534.

Details

Redox score ?
94
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
4
% buried
19
Peptide accession
Q15910
Residue number A
530
Residue number B
534
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 530 of Histone-lysine N-methyltransferase EZH2

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 534 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 562 and 571.

Details

Redox score ?
92
PDB code
5ij8
Structure name
structure of the primary oncogenic mutant y641n hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
21
Peptide accession
Q15910
Residue number A
562
Residue number B
571
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 562 of Histone-lysine N-methyltransferase EZH2

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 571 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 562 and 566.

Details

Redox score ?
92
PDB code
5ij8
Structure name
structure of the primary oncogenic mutant y641n hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
24
Peptide accession
Q15910
Residue number A
562
Residue number B
566
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 562 of Histone-lysine N-methyltransferase EZH2

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 566 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 324 and 463.

Details

Redox score ?
91
PDB code
5hyn
Structure name
structure of human polycomb repressive complex 2 (prc2) with oncogenic histone h3k27m peptide
Structure deposition date
2016-02-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
1
% buried
61
Peptide accession
Q15910
Residue number A
324
Residue number B
463
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 324 of Histone-lysine N-methyltransferase EZH2

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 463 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 560 and 571.

Details

Redox score ?
90
PDB code
5ij8
Structure name
structure of the primary oncogenic mutant y641n hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
4
% buried
34
Peptide accession
Q15910
Residue number A
560
Residue number B
571
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 560 of Histone-lysine N-methyltransferase EZH2

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 571 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 536 and 547.

Details

Redox score ?
90
PDB code
5hyn
Structure name
structure of human polycomb repressive complex 2 (prc2) with oncogenic histone h3k27m peptide
Structure deposition date
2016-02-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
1
% buried
67
Peptide accession
Q15910
Residue number A
536
Residue number B
547
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 536 of Histone-lysine N-methyltransferase EZH2

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 547 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 523 and 534.

Details

Redox score ?
90
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
4
% buried
32
Peptide accession
Q15910
Residue number A
523
Residue number B
534
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 523 of Histone-lysine N-methyltransferase EZH2

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 534 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 530 and 549.

Details

Redox score ?
90
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
5
% buried
30
Peptide accession
Q15910
Residue number A
530
Residue number B
549
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 530 of Histone-lysine N-methyltransferase EZH2

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 549 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 560 and 562.

Details

Redox score ?
89
PDB code
5ij8
Structure name
structure of the primary oncogenic mutant y641n hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
24
Peptide accession
Q15910
Residue number A
560
Residue number B
562
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 560 of Histone-lysine N-methyltransferase EZH2

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 Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 320 and 452.

Details

Redox score ?
89
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
3
% buried
44
Peptide accession
Q15910
Residue number A
320
Residue number B
452
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 320 of Histone-lysine N-methyltransferase EZH2

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 452 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 566 and 571.

Details

Redox score ?
89
PDB code
5ij8
Structure name
structure of the primary oncogenic mutant y641n hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
36
Peptide accession
Q15910
Residue number A
566
Residue number B
571
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 566 of Histone-lysine N-methyltransferase EZH2

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 571 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 534 and 536.

Details

Redox score ?
88
PDB code
5hyn
Structure name
structure of human polycomb repressive complex 2 (prc2) with oncogenic histone h3k27m peptide
Structure deposition date
2016-02-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
4
% buried
40
Peptide accession
Q15910
Residue number A
534
Residue number B
536
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 534 of Histone-lysine N-methyltransferase EZH2

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 536 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 534 and 543 (539 and 548 respectively in this structure).

Details

Redox score ?
88
PDB code
4mi5
Structure name
crystal structure of the ezh2 set domain
Structure deposition date
2013-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
4
% buried
12
Peptide accession
Q15910
Residue number A
534
Residue number B
543
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 534 of Histone-lysine N-methyltransferase EZH2

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 543 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 566 and 588.

Details

Redox score ?
87
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
4
% buried
50
Peptide accession
Q15910
Residue number A
566
Residue number B
588
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 566 of Histone-lysine N-methyltransferase EZH2

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 588 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 560 and 588.

Details

Redox score ?
87
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
4
% buried
44
Peptide accession
Q15910
Residue number A
560
Residue number B
588
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 560 of Histone-lysine N-methyltransferase EZH2

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 588 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 571 and 580 (576 and 585 respectively in this structure).

Details

Redox score ?
87
PDB code
4mi5
Structure name
crystal structure of the ezh2 set domain
Structure deposition date
2013-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
2
% buried
46
Peptide accession
Q15910
Residue number A
571
Residue number B
580
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 571 of Histone-lysine N-methyltransferase EZH2

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 580 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 452 and 463.

Details

Redox score ?
86
PDB code
5ij7
Structure name
structure of hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q15910
Residue number A
452
Residue number B
463
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 452 of Histone-lysine N-methyltransferase EZH2

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 463 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 530 and 553 (535 and 558 respectively in this structure).

Details

Redox score ?
85
PDB code
4mi5
Structure name
crystal structure of the ezh2 set domain
Structure deposition date
2013-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
6
Peptide accession
Q15910
Residue number A
530
Residue number B
553
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 530 of Histone-lysine N-methyltransferase EZH2

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 553 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 580 and 588.

Details

Redox score ?
85
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
4
% buried
nan
Peptide accession
Q15910
Residue number A
580
Residue number B
588
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 580 of Histone-lysine N-methyltransferase EZH2

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 588 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 286 and 289.

Details

Redox score ?
82
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
nan
Peptide accession
Q15910
Residue number A
286
Residue number B
289
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 286 of Histone-lysine N-methyltransferase EZH2

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 289 of Histone-lysine N-methyltransferase EZH2

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 Isoform 2 of Histone-lysine N-methyltransferase EZH2 between cysteines 548 and 552 (561 and 565 respectively in this structure).

Details

Redox score ?
82
PDB code
7at8
Structure name
histone h3 recognition by nucleosome-bound prc2 subunit ezh2
Structure deposition date
2020-10-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
nan
Peptide accession
Q15910-2
Residue number A
548
Residue number B
552
Peptide name
Isoform 2 of Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 548 of Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 552 of Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 566 and 585.

Details

Redox score ?
81
PDB code
6wkr
Structure name
prc2-aebp2-jarid2 bound to h2ak119ub1 nucleosome
Structure deposition date
2020-04-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15910
Residue number A
566
Residue number B
585
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 566 of Histone-lysine N-methyltransferase EZH2

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 585 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 560 and 585.

Details

Redox score ?
81
PDB code
5hyn
Structure name
structure of human polycomb repressive complex 2 (prc2) with oncogenic histone h3k27m peptide
Structure deposition date
2016-02-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
nan
Peptide accession
Q15910
Residue number A
560
Residue number B
585
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 560 of Histone-lysine N-methyltransferase EZH2

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 585 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 286 and 294.

Details

Redox score ?
81
PDB code
5ij8
Structure name
structure of the primary oncogenic mutant y641n hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
5
% buried
nan
Peptide accession
Q15910
Residue number A
286
Residue number B
294
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 286 of Histone-lysine N-methyltransferase EZH2

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 294 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 549 and 553.

Details

Redox score ?
81
PDB code
6wkr
Structure name
prc2-aebp2-jarid2 bound to h2ak119ub1 nucleosome
Structure deposition date
2020-04-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15910
Residue number A
549
Residue number B
553
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 549 of Histone-lysine N-methyltransferase EZH2

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 553 of Histone-lysine N-methyltransferase EZH2

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 Isoform 2 of Histone-lysine N-methyltransferase EZH2 between cysteines 548 and 558 (561 and 571 respectively in this structure).

Details

Redox score ?
81
PDB code
7at8
Structure name
histone h3 recognition by nucleosome-bound prc2 subunit ezh2
Structure deposition date
2020-10-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
nan
Peptide accession
Q15910-2
Residue number A
548
Residue number B
558
Peptide name
Isoform 2 of Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 548 of Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 558 of Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 560 and 566.

Details

Redox score ?
80
PDB code
5ij8
Structure name
structure of the primary oncogenic mutant y641n hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
38
Peptide accession
Q15910
Residue number A
560
Residue number B
566
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 560 of Histone-lysine N-methyltransferase EZH2

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 566 of Histone-lysine N-methyltransferase EZH2

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 Isoform 2 of Histone-lysine N-methyltransferase EZH2 between cysteines 528 and 535 (541 and 548 respectively in this structure).

Details

Redox score ?
80
PDB code
7at8
Structure name
histone h3 recognition by nucleosome-bound prc2 subunit ezh2
Structure deposition date
2020-10-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
19
Peptide accession
Q15910-2
Residue number A
528
Residue number B
535
Peptide name
Isoform 2 of Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 528 of Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 320 and 324.

Details

Redox score ?
80
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
7
% buried
19
Peptide accession
Q15910
Residue number A
320
Residue number B
324
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 320 of Histone-lysine N-methyltransferase EZH2

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 324 of Histone-lysine N-methyltransferase EZH2

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 Isoform 2 of Histone-lysine N-methyltransferase EZH2 between cysteines 552 and 554 (565 and 567 respectively in this structure).

Details

Redox score ?
80
PDB code
7at8
Structure name
histone h3 recognition by nucleosome-bound prc2 subunit ezh2
Structure deposition date
2020-10-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
38
Peptide accession
Q15910-2
Residue number A
552
Residue number B
554
Peptide name
Isoform 2 of Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 552 of Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 580 and 585.

Details

Redox score ?
79
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
82
Minimum pKa ?
8
% buried
nan
Peptide accession
Q15910
Residue number A
580
Residue number B
585
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 580 of Histone-lysine N-methyltransferase EZH2

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 585 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 523 and 543.

Details

Redox score ?
78
PDB code
5hyn
Structure name
structure of human polycomb repressive complex 2 (prc2) with oncogenic histone h3k27m peptide
Structure deposition date
2016-02-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
79
Minimum pKa ?
7
% buried
60
Peptide accession
Q15910
Residue number A
523
Residue number B
543
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 523 of Histone-lysine N-methyltransferase EZH2

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 543 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 571 and 573 (576 and 578 respectively in this structure).

Details

Redox score ?
78
PDB code
4mi5
Structure name
crystal structure of the ezh2 set domain
Structure deposition date
2013-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
7
% buried
44
Peptide accession
Q15910
Residue number A
571
Residue number B
573
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 571 of Histone-lysine N-methyltransferase EZH2

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 573 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 547 and 553.

Details

Redox score ?
78
PDB code
5ij7
Structure name
structure of hs/acprc2 in complex with a pyridone inhibitor
Structure deposition date
2016-03-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
1
% buried
42
Peptide accession
Q15910
Residue number A
547
Residue number B
553
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 547 of Histone-lysine N-methyltransferase EZH2

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 553 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 573 and 580.

Details

Redox score ?
77
PDB code
6wkr
Structure name
prc2-aebp2-jarid2 bound to h2ak119ub1 nucleosome
Structure deposition date
2020-04-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15910
Residue number A
573
Residue number B
580
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 573 of Histone-lysine N-methyltransferase EZH2

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 580 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 566 and 601.

Details

Redox score ?
76
PDB code
5hyn
Structure name
structure of human polycomb repressive complex 2 (prc2) with oncogenic histone h3k27m peptide
Structure deposition date
2016-02-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
62
Peptide accession
Q15910
Residue number A
566
Residue number B
601
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 566 of Histone-lysine N-methyltransferase EZH2

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 601 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 523 and 536.

Details

Redox score ?
76
PDB code
5hyn
Structure name
structure of human polycomb repressive complex 2 (prc2) with oncogenic histone h3k27m peptide
Structure deposition date
2016-02-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
50
Peptide accession
Q15910
Residue number A
523
Residue number B
536
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 523 of Histone-lysine N-methyltransferase EZH2

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 536 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 523 and 549.

Details

Redox score ?
76
PDB code
5ls6
Structure name
structure of human polycomb repressive complex 2 (prc2) with inhibitor
Structure deposition date
2016-08-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
7
% buried
40
Peptide accession
Q15910
Residue number A
523
Residue number B
549
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 523 of Histone-lysine N-methyltransferase EZH2

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 549 of Histone-lysine N-methyltransferase EZH2

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 EZH2 between cysteines 588 and 601.

Details

Redox score ?
76
PDB code
5hyn
Structure name
structure of human polycomb repressive complex 2 (prc2) with oncogenic histone h3k27m peptide
Structure deposition date
2016-02-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
62
Peptide accession
Q15910
Residue number A
588
Residue number B
601
Peptide name
Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 588 of Histone-lysine N-methyltransferase EZH2

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 601 of Histone-lysine N-methyltransferase EZH2

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 Isoform 2 of Histone-lysine N-methyltransferase EZH2 between cysteines 548 and 554 (561 and 567 respectively in this structure).

Details

Redox score ?
75
PDB code
7at8
Structure name
histone h3 recognition by nucleosome-bound prc2 subunit ezh2
Structure deposition date
2020-10-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
nan
Peptide accession
Q15910-2
Residue number A
548
Residue number B
554
Peptide name
Isoform 2 of Histone-lysine N-methyltransferase EZH2

Ligandability

Cysteine 548 of Isoform 2 of Histone-lysine N-methyltransferase EZH2

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 Isoform 2 of Histone-lysine N-methyltransferase EZH2

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.

If this tool was useful for finding a disulphide, please cite: