ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Structural maintenance of chromosomes protein 3

Intramolecular
Cysteine 633 and cysteine 650
Cysteine 542 and cysteine 549 L
Cysteine 549 and cysteine 633
A redox-regulated disulphide may form within Structural maintenance of chromosomes protein 3 between cysteines 633 and 650.

Details

Redox score ?
77
PDB code
7dg5
Structure name
crystal structure of mouse smc1-smc3 hinge domain containing a d574y mutation
Structure deposition date
2020-11-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
82
Peptide accession
Q9CW03
Residue number A
633
Residue number B
650
Peptide name
Structural maintenance of chromosomes protein 3

Ligandability

Cysteine 633 of Structural maintenance of chromosomes protein 3

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 650 of Structural maintenance of chromosomes protein 3

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 protein 3 between cysteines 542 and 549 (541 and 548 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6wg6
Structure name
crystal structure of human smc1-smc3 hinge domain heterodimer in north-open conformation
Structure deposition date
2020-04-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
66
Peptide accession
Q9UQE7
Residue number A
542
Residue number B
549
Peptide name
Structural maintenance of chromosomes protein 3

Ligandability

Cysteine 542 of Structural maintenance of chromosomes protein 3

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 549 of Structural maintenance of chromosomes protein 3

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 protein 3 between cysteines 549 and 633. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6wg4
Structure name
crystal structure of human smc1-smc3 hinge domain heterodimer in south-open conformation
Structure deposition date
2020-04-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
49
Peptide accession
Q9UQE7
Residue number A
549
Residue number B
633
Peptide name
Structural maintenance of chromosomes protein 3

Ligandability

Cysteine 549 of Structural maintenance of chromosomes protein 3

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 633 of Structural maintenance of chromosomes protein 3

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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