ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Stromal membrane-associated protein 1

Intramolecular
Cysteine 33 and cysteine 36 L
Cysteine 36 and cysteine 53 L
Cysteine 33 and cysteine 56 L
Cysteine 53 and cysteine 56
Cysteine 33 and cysteine 53 L
Cysteine 36 and cysteine 56 L
A redox-regulated disulphide may form within Stromal membrane-associated protein 1 between cysteines 33 and 36 (32 and 35 respectively in this structure).

Details

Redox score ?
85
PDB code
2crr
Structure name
solution structure of arfgap domain from human smap1
Structure deposition date
2005-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
3
% buried
66
Peptide accession
Q6PK24
Residue number A
33
Residue number B
36
Peptide name
Stromal membrane-associated protein 1

Ligandability

Cysteine 33 of Stromal membrane-associated protein 1

Cysteine 36 of Stromal membrane-associated protein 1

A redox-regulated disulphide may form within Stromal membrane-associated protein 1 between cysteines 36 and 53 (35 and 52 respectively in this structure).

Details

Redox score ?
85
PDB code
2crr
Structure name
solution structure of arfgap domain from human smap1
Structure deposition date
2005-05-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
46
Peptide accession
Q6PK24
Residue number A
36
Residue number B
53
Peptide name
Stromal membrane-associated protein 1

Ligandability

Cysteine 36 of Stromal membrane-associated protein 1

Cysteine 53 of Stromal membrane-associated protein 1

A redox-regulated disulphide may form within Stromal membrane-associated protein 1 between cysteines 33 and 56 (32 and 55 respectively in this structure).

Details

Redox score ?
83
PDB code
2crr
Structure name
solution structure of arfgap domain from human smap1
Structure deposition date
2005-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
3
% buried
80
Peptide accession
Q6PK24
Residue number A
33
Residue number B
56
Peptide name
Stromal membrane-associated protein 1

Ligandability

Cysteine 33 of Stromal membrane-associated protein 1

Cysteine 56 of Stromal membrane-associated protein 1

A redox-regulated disulphide may form within Stromal membrane-associated protein 1 between cysteines 53 and 56 (52 and 55 respectively in this structure).

Details

Redox score ?
83
PDB code
2crr
Structure name
solution structure of arfgap domain from human smap1
Structure deposition date
2005-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
5
% buried
60
Peptide accession
Q6PK24
Residue number A
53
Residue number B
56
Peptide name
Stromal membrane-associated protein 1

Ligandability

Cysteine 53 of Stromal membrane-associated protein 1

Cysteine 56 of Stromal membrane-associated protein 1

A redox-regulated disulphide may form within Stromal membrane-associated protein 1 between cysteines 33 and 53 (32 and 52 respectively in this structure).

Details

Redox score ?
83
PDB code
2crr
Structure name
solution structure of arfgap domain from human smap1
Structure deposition date
2005-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
3
% buried
68
Peptide accession
Q6PK24
Residue number A
33
Residue number B
53
Peptide name
Stromal membrane-associated protein 1

Ligandability

Cysteine 33 of Stromal membrane-associated protein 1

Cysteine 53 of Stromal membrane-associated protein 1

A redox-regulated disulphide may form within Stromal membrane-associated protein 1 between cysteines 36 and 56 (35 and 55 respectively in this structure).

Details

Redox score ?
74
PDB code
2crr
Structure name
solution structure of arfgap domain from human smap1
Structure deposition date
2005-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
58
Peptide accession
Q6PK24
Residue number A
36
Residue number B
56
Peptide name
Stromal membrane-associated protein 1

Ligandability

Cysteine 36 of Stromal membrane-associated protein 1

Cysteine 56 of Stromal membrane-associated protein 1

If this tool was useful for finding a disulphide, please cite: