ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Nucleotide exchange factor SIL1

Intramolecular
Cysteine 25 and cysteine 152
Cysteine 25 and cysteine 294
Cysteine 294 and cysteine 189
A redox-regulated disulphide may form within Nucleotide exchange factor SIL1 between cysteines 25 and 152 (124 and 152 respectively in this structure).

Details

Redox score ?
62
PDB code
6lbn
Structure name
structure of sil1-bound fem1c
Structure deposition date
2019-11-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
96
Minimum pKa ?
8
% buried
100
Peptide accession
Q9H173
Residue number A
25
Residue number B
152
Peptide name
Nucleotide exchange factor SIL1

Ligandability

Cysteine 25 of Nucleotide exchange factor SIL1

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 152 of Nucleotide exchange factor SIL1

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 152 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Nucleotide exchange factor SIL1 between cysteines 25 and 294 (124 and 157 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
16
PDB code
6ley
Structure name
structure of sil1g bound fem1c
Structure deposition date
2019-11-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
17
% buried
100
Peptide accession
Q9H173
Residue number A
25
Residue number B
294
Peptide name
Nucleotide exchange factor SIL1

Ligandability

Cysteine 25 of Nucleotide exchange factor SIL1

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 294 of Nucleotide exchange factor SIL1

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.

Uncertain whether structure cysteine 157 has been assigned to correct residue.
A redox-regulated disulphide may form within Nucleotide exchange factor SIL1 between cysteines 294 and 189 (157 and 189 respectively in this structure).

Details

Redox score ?
nan
PDB code
6lbn
Structure name
structure of sil1-bound fem1c
Structure deposition date
2019-11-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
98
Peptide accession
Q9H173
Residue number A
294
Residue number B
189
Peptide name
Nucleotide exchange factor SIL1

Ligandability

Cysteine 294 of Nucleotide exchange factor SIL1

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 189 of Nucleotide exchange factor SIL1

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.

Uncertain whether structure cysteine 157 has been assigned to correct residue.
Cysteine 189 in protein B could not be asigned to a Uniprot residue.
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