ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Actin-histidine N-methyltransferase

Intramolecular
Cysteine 277 and cysteine 297
Cysteine 295 and cysteine 297
Cysteine 277 and cysteine 295
A redox-regulated disulphide may form within Actin-histidine N-methyltransferase between cysteines 277 and 297 (276 and 296 respectively in this structure).

Details

Redox score ?
64
PDB code
3smt
Structure name
crystal structure of human set domain-containing protein3
Structure deposition date
2011-06-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q86TU7
Residue number A
277
Residue number B
297
Peptide name
Actin-histidine N-methyltransferase

Ligandability

Cysteine 277 of Actin-histidine N-methyltransferase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 297 of Actin-histidine N-methyltransferase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Actin-histidine N-methyltransferase between cysteines 295 and 297. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6icv
Structure name
structure of setd3 bound to sah and unmodified actin
Structure deposition date
2018-09-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
100
Peptide accession
Q86TU7
Residue number A
295
Residue number B
297
Peptide name
Actin-histidine N-methyltransferase

Ligandability

Cysteine 295 of Actin-histidine N-methyltransferase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 297 of Actin-histidine N-methyltransferase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Actin-histidine N-methyltransferase between cysteines 277 and 295 (276 and 294 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
7w29
Structure name
crystal structure of setd3-sah in complex with betaa-orn73 peptide
Structure deposition date
2021-11-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
100
Peptide accession
Q86TU7
Residue number A
277
Residue number B
295
Peptide name
Actin-histidine N-methyltransferase

Ligandability

Cysteine 277 of Actin-histidine N-methyltransferase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 295 of Actin-histidine N-methyltransferase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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