ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Intramolecular
Cysteine 1711 and cysteine 1824
Cysteine 59 and cysteine 61
Cysteine 505 and cysteine 566 L
A redox-regulated disulphide may form within Structural maintenance of chromosomes flexible hinge domain-containing protein 1 between cysteines 1711 and 1824.

Details

Redox score ?
81
PDB code
6n64
Structure name
crystal structure of mouse smchd1 hinge domain
Structure deposition date
2018-11-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
29
Peptide accession
Q6P5D8
Residue number A
1711
Residue number B
1824
Peptide name
Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Ligandability

Cysteine 1711 of Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 1824 of Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Structural maintenance of chromosomes flexible hinge domain-containing protein 1 between cysteines 59 and 61. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6mw7
Structure name
crystal structure of atpase module of smchd1 bound to atp
Structure deposition date
2018-10-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
0
Peptide accession
A6NHR9
Residue number A
59
Residue number B
61
Peptide name
Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Ligandability

Cysteine 59 of Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 61 of Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Structural maintenance of chromosomes flexible hinge domain-containing protein 1 between cysteines 505 and 566. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6mw7
Structure name
crystal structure of atpase module of smchd1 bound to atp
Structure deposition date
2018-10-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
62
Peptide accession
A6NHR9
Residue number A
505
Residue number B
566
Peptide name
Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Ligandability

Cysteine 505 of Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 566 of Structural maintenance of chromosomes flexible hinge domain-containing protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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