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Histone-lysine N-methyltransferase NSD3

Intramolecular
Cysteine 1336 and cysteine 1341
Cysteine 1275 and cysteine 1280
Cysteine 1378 and cysteine 1405
Cysteine 1273 and cysteine 1275
Cysteine 1367 and cysteine 1386
Cysteine 1273 and cysteine 1280
Cysteine 1108 and cysteine 1123
Cysteine 1370 and cysteine 1386
Cysteine 1367 and cysteine 1370
Cysteine 1324 and cysteine 1327
More...
Cysteine 1108 and cysteine 1114
Cysteine 1336 and cysteine 1362
Cysteine 1108 and cysteine 1128
Cysteine 1100 and cysteine 1114
Cysteine 1128 and cysteine 1134
Cysteine 1324 and cysteine 1349
Cysteine 1327 and cysteine 1349
Cysteine 1226 and cysteine 1280
Cysteine 1098 and cysteine 1114
Cysteine 1378 and cysteine 1381
Cysteine 1098 and cysteine 1100
Cysteine 1100 and cysteine 1108
Cysteine 1341 and cysteine 1362
Cysteine 1098 and cysteine 1108
Cysteine 1226 and cysteine 1273
Cysteine 1098 and cysteine 1128
Cysteine 1381 and cysteine 1405
Cysteine 1108 and cysteine 1134
Cysteine 1123 and cysteine 1134
Cysteine 1226 and cysteine 1275
Cysteine 1378 and cysteine 1404
Cysteine 1123 and cysteine 1128
Cysteine 1100 and cysteine 1123
Cysteine 1114 and cysteine 1123
Cysteine 1098 and cysteine 1123
Cysteine 1114 and cysteine 1128
Cysteine 1098 and cysteine 1134
Cysteine 1100 and cysteine 1128
Cysteine 1114 and cysteine 1134
Cysteine 1404 and cysteine 1405
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase NSD3 between cysteines 1336 and 1341.

Details

Redox score ?
90
PDB code
4gng
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains complexed with h3k9me3 peptide
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
3
% buried
43
Peptide accession
Q9BZ95
Residue number A
1336
Residue number B
1341
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1336 of Histone-lysine N-methyltransferase NSD3

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 1341 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1275 and 1280.

Details

Redox score ?
89
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
10
Peptide accession
Q9BZ95
Residue number A
1275
Residue number B
1280
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1275 of Histone-lysine N-methyltransferase NSD3

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 1280 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1378 and 1405.

Details

Redox score ?
88
PDB code
4gng
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains complexed with h3k9me3 peptide
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
3
% buried
38
Peptide accession
Q9BZ95
Residue number A
1378
Residue number B
1405
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1378 of Histone-lysine N-methyltransferase NSD3

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 1405 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1273 and 1275.

Details

Redox score ?
87
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
26
Peptide accession
Q9BZ95
Residue number A
1273
Residue number B
1275
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1273 of Histone-lysine N-methyltransferase NSD3

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 1275 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1367 and 1386.

Details

Redox score ?
87
PDB code
4gnd
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
0
Peptide accession
Q9BZ95
Residue number A
1367
Residue number B
1386
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1367 of Histone-lysine N-methyltransferase NSD3

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 1386 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1273 and 1280.

Details

Redox score ?
86
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
16
Peptide accession
Q9BZ95
Residue number A
1273
Residue number B
1280
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1273 of Histone-lysine N-methyltransferase NSD3

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 1280 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1108 and 1123.

Details

Redox score ?
86
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
2
% buried
48
Peptide accession
Q9BZ95
Residue number A
1108
Residue number B
1123
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1108 of Histone-lysine N-methyltransferase NSD3

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 1123 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1370 and 1386.

Details

Redox score ?
85
PDB code
4gng
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains complexed with h3k9me3 peptide
Structure deposition date
2012-08-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
Q9BZ95
Residue number A
1370
Residue number B
1386
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1370 of Histone-lysine N-methyltransferase NSD3

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 1386 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1367 and 1370.

Details

Redox score ?
85
PDB code
4gnd
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
0
Peptide accession
Q9BZ95
Residue number A
1367
Residue number B
1370
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1367 of Histone-lysine N-methyltransferase NSD3

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 1370 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1324 and 1327.

Details

Redox score ?
81
PDB code
4gng
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains complexed with h3k9me3 peptide
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
34
Peptide accession
Q9BZ95
Residue number A
1324
Residue number B
1327
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1324 of Histone-lysine N-methyltransferase NSD3

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 1327 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1108 and 1114.

Details

Redox score ?
80
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
40
Peptide accession
Q9BZ95
Residue number A
1108
Residue number B
1114
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1108 of Histone-lysine N-methyltransferase NSD3

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 1114 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1336 and 1362.

Details

Redox score ?
79
PDB code
4gnd
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
48
Peptide accession
Q9BZ95
Residue number A
1336
Residue number B
1362
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1336 of Histone-lysine N-methyltransferase NSD3

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 1362 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1108 and 1128.

Details

Redox score ?
79
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
36
Peptide accession
Q9BZ95
Residue number A
1108
Residue number B
1128
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1108 of Histone-lysine N-methyltransferase NSD3

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 1128 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1100 and 1114.

Details

Redox score ?
78
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1100
Residue number B
1114
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1100 of Histone-lysine N-methyltransferase NSD3

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 1114 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1128 and 1134.

Details

Redox score ?
78
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
44
Peptide accession
Q9BZ95
Residue number A
1128
Residue number B
1134
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1128 of Histone-lysine N-methyltransferase NSD3

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 1134 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1324 and 1349.

Details

Redox score ?
77
PDB code
4gng
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains complexed with h3k9me3 peptide
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
35
Peptide accession
Q9BZ95
Residue number A
1324
Residue number B
1349
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1324 of Histone-lysine N-methyltransferase NSD3

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 1349 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1327 and 1349.

Details

Redox score ?
77
PDB code
4gnd
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
0
Peptide accession
Q9BZ95
Residue number A
1327
Residue number B
1349
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1327 of Histone-lysine N-methyltransferase NSD3

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 1349 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1226 and 1280.

Details

Redox score ?
77
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1226
Residue number B
1280
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1226 of Histone-lysine N-methyltransferase NSD3

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 1280 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1098 and 1114.

Details

Redox score ?
76
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1098
Residue number B
1114
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1098 of Histone-lysine N-methyltransferase NSD3

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 1114 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1378 and 1381.

Details

Redox score ?
76
PDB code
4gnd
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
44
Peptide accession
Q9BZ95
Residue number A
1378
Residue number B
1381
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1378 of Histone-lysine N-methyltransferase NSD3

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 1381 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1098 and 1100.

Details

Redox score ?
76
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1098
Residue number B
1100
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1098 of Histone-lysine N-methyltransferase NSD3

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 1100 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1100 and 1108.

Details

Redox score ?
76
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1100
Residue number B
1108
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1100 of Histone-lysine N-methyltransferase NSD3

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 1108 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1341 and 1362.

Details

Redox score ?
75
PDB code
4gng
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains complexed with h3k9me3 peptide
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
58
Peptide accession
Q9BZ95
Residue number A
1341
Residue number B
1362
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1341 of Histone-lysine N-methyltransferase NSD3

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 1362 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1098 and 1108.

Details

Redox score ?
75
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1098
Residue number B
1108
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1098 of Histone-lysine N-methyltransferase NSD3

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 1108 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1226 and 1273.

Details

Redox score ?
75
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1226
Residue number B
1273
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1226 of Histone-lysine N-methyltransferase NSD3

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 1273 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1098 and 1128.

Details

Redox score ?
75
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1098
Residue number B
1128
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1098 of Histone-lysine N-methyltransferase NSD3

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 1128 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1381 and 1405.

Details

Redox score ?
74
PDB code
4gnd
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains
Structure deposition date
2012-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
37
Peptide accession
Q9BZ95
Residue number A
1381
Residue number B
1405
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1381 of Histone-lysine N-methyltransferase NSD3

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 1405 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1108 and 1134.

Details

Redox score ?
74
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1108
Residue number B
1134
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1108 of Histone-lysine N-methyltransferase NSD3

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 1134 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1123 and 1134.

Details

Redox score ?
74
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1123
Residue number B
1134
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1123 of Histone-lysine N-methyltransferase NSD3

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 1134 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1226 and 1275.

Details

Redox score ?
74
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1226
Residue number B
1275
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1226 of Histone-lysine N-methyltransferase NSD3

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 1275 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1378 and 1404.

Details

Redox score ?
73
PDB code
4gng
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains complexed with h3k9me3 peptide
Structure deposition date
2012-08-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
3
% buried
40
Peptide accession
Q9BZ95
Residue number A
1378
Residue number B
1404
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1378 of Histone-lysine N-methyltransferase NSD3

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 1404 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1123 and 1128.

Details

Redox score ?
73
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1123
Residue number B
1128
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1123 of Histone-lysine N-methyltransferase NSD3

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 1128 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1100 and 1123.

Details

Redox score ?
72
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
2
% buried
36
Peptide accession
Q9BZ95
Residue number A
1100
Residue number B
1123
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1100 of Histone-lysine N-methyltransferase NSD3

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 1123 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1114 and 1123.

Details

Redox score ?
72
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1114
Residue number B
1123
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1114 of Histone-lysine N-methyltransferase NSD3

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 1123 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1098 and 1123.

Details

Redox score ?
69
PDB code
5upd
Structure name
methyltransferase domain of human wolf-hirschhorn syndrome candidate 1-like protein 1 (whsc1l1)
Structure deposition date
2017-02-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ95
Residue number A
1098
Residue number B
1123
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1098 of Histone-lysine N-methyltransferase NSD3

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 1123 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1114 and 1128.

Details

Redox score ?
68
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
39
Peptide accession
Q9BZ95
Residue number A
1114
Residue number B
1128
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1114 of Histone-lysine N-methyltransferase NSD3

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 1128 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1098 and 1134.

Details

Redox score ?
67
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
41
Peptide accession
Q9BZ95
Residue number A
1098
Residue number B
1134
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1098 of Histone-lysine N-methyltransferase NSD3

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 1134 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1100 and 1128.

Details

Redox score ?
66
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
26
Peptide accession
Q9BZ95
Residue number A
1100
Residue number B
1128
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1100 of Histone-lysine N-methyltransferase NSD3

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 1128 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1114 and 1134.

Details

Redox score ?
64
PDB code
6cen
Structure name
crystal structure of whsc1l1 in complex with inhibitor pep21
Structure deposition date
2018-02-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
48
Peptide accession
Q9BZ95
Residue number A
1114
Residue number B
1134
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1114 of Histone-lysine N-methyltransferase NSD3

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 1134 of Histone-lysine N-methyltransferase NSD3

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 NSD3 between cysteines 1404 and 1405. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
4gng
Structure name
crystal structure of nsd3 tandem phd5-c5hch domains complexed with h3k9me3 peptide
Structure deposition date
2012-08-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
28
Peptide accession
Q9BZ95
Residue number A
1404
Residue number B
1405
Peptide name
Histone-lysine N-methyltransferase NSD3

Ligandability

Cysteine 1404 of Histone-lysine N-methyltransferase NSD3

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 1405 of Histone-lysine N-methyltransferase NSD3

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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