ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone-lysine N-methyltransferase KMT5B

Intramolecular
Cysteine 322 and cysteine 325
Cysteine 320 and cysteine 322
Cysteine 275 and cysteine 321
Cysteine 275 and cysteine 324
Cysteine 319 and cysteine 324
Cysteine 276 and cysteine 320
Cysteine 279 and cysteine 305
Cysteine 279 and cysteine 290
Cysteine 290 and cysteine 305
A redox-regulated disulphide may form within Histone-lysine N-methyltransferase KMT5B between cysteines 322 and 325 (313 and 316 respectively in this structure).

Details

Redox score ?
86
PDB code
4bup
Structure name
a novel route to product specificity in the suv4-20 family of histone h4k20 methyltransferases
Structure deposition date
2013-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
4
% buried
38
Peptide accession
Q3U8K7
Residue number A
322
Residue number B
325
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 322 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 325 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B between cysteines 320 and 322 (311 and 313 respectively in this structure).

Details

Redox score ?
86
PDB code
4bup
Structure name
a novel route to product specificity in the suv4-20 family of histone h4k20 methyltransferases
Structure deposition date
2013-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
4
% buried
46
Peptide accession
Q3U8K7
Residue number A
320
Residue number B
322
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 320 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 322 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B between cysteines 275 and 321.

Details

Redox score ?
83
PDB code
3s8p
Structure name
crystal structure of the set domain of human histone-lysine n- methyltransferase suv420h1 in complex with s-adenosyl-l-methionine
Structure deposition date
2011-05-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
4
% buried
44
Peptide accession
Q4FZB7
Residue number A
275
Residue number B
321
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 275 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 321 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B between cysteines 275 and 324.

Details

Redox score ?
80
PDB code
3s8p
Structure name
crystal structure of the set domain of human histone-lysine n- methyltransferase suv420h1 in complex with s-adenosyl-l-methionine
Structure deposition date
2011-05-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
30
Peptide accession
Q4FZB7
Residue number A
275
Residue number B
324
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 275 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B between cysteines 319 and 324.

Details

Redox score ?
75
PDB code
5wbv
Structure name
crystal structure of the set domain of human suv420h1 in complex with inhibitor
Structure deposition date
2017-06-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4FZB7
Residue number A
319
Residue number B
324
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 319 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B between cysteines 276 and 320 (267 and 311 respectively in this structure).

Details

Redox score ?
71
PDB code
4bup
Structure name
a novel route to product specificity in the suv4-20 family of histone h4k20 methyltransferases
Structure deposition date
2013-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
45
Peptide accession
Q3U8K7
Residue number A
276
Residue number B
320
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 276 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 320 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B between cysteines 279 and 305.

Details

Redox score ?
65
PDB code
5wbv
Structure name
crystal structure of the set domain of human suv420h1 in complex with inhibitor
Structure deposition date
2017-06-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4FZB7
Residue number A
279
Residue number B
305
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 279 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 305 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B between cysteines 279 and 290. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3s8p
Structure name
crystal structure of the set domain of human histone-lysine n- methyltransferase suv420h1 in complex with s-adenosyl-l-methionine
Structure deposition date
2011-05-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
58
Peptide accession
Q4FZB7
Residue number A
279
Residue number B
290
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 279 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 290 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 KMT5B between cysteines 290 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5wbv
Structure name
crystal structure of the set domain of human suv420h1 in complex with inhibitor
Structure deposition date
2017-06-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q4FZB7
Residue number A
290
Residue number B
305
Peptide name
Histone-lysine N-methyltransferase KMT5B

Ligandability

Cysteine 290 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 305 of Histone-lysine N-methyltransferase KMT5B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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