ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Klotho

Intramolecular
Cysteine 910 and cysteine 973
Cysteine 572 and cysteine 621
Cysteine 521 and cysteine 970
Cysteine 970 and cysteine 973
Cysteine 521 and cysteine 963
Cysteine 910 and cysteine 970
Cysteine 521 and cysteine 973
A redox-regulated disulphide may form within Klotho between cysteines 910 and 973.

Details

Redox score ?
82
PDB code
5w21
Structure name
crystal structure of a 1:1:1 fgf23-fgfr1c-aklotho ternary complex
Structure deposition date
2017-06-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UEF7
Residue number A
910
Residue number B
973
Peptide name
Klotho

Ligandability

Cysteine 910 of Klotho

Cysteine 973 of Klotho

A redox-regulated disulphide may form within Klotho between cysteines 572 and 621.

Details

Redox score ?
82
PDB code
5w21
Structure name
crystal structure of a 1:1:1 fgf23-fgfr1c-aklotho ternary complex
Structure deposition date
2017-06-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UEF7
Residue number A
572
Residue number B
621
Peptide name
Klotho

Ligandability

Cysteine 572 of Klotho

Cysteine 621 of Klotho

A redox-regulated disulphide may form within Klotho between cysteines 521 and 970.

Details

Redox score ?
76
PDB code
5w21
Structure name
crystal structure of a 1:1:1 fgf23-fgfr1c-aklotho ternary complex
Structure deposition date
2017-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
8
Peptide accession
Q9UEF7
Residue number A
521
Residue number B
970
Peptide name
Klotho

Ligandability

Cysteine 521 of Klotho

Cysteine 970 of Klotho

A redox-regulated disulphide may form within Klotho between cysteines 970 and 973. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5w21
Structure name
crystal structure of a 1:1:1 fgf23-fgfr1c-aklotho ternary complex
Structure deposition date
2017-06-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9UEF7
Residue number A
970
Residue number B
973
Peptide name
Klotho

Ligandability

Cysteine 970 of Klotho

Cysteine 973 of Klotho

A redox-regulated disulphide may form within Klotho between cysteines 521 and 963. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5w21
Structure name
crystal structure of a 1:1:1 fgf23-fgfr1c-aklotho ternary complex
Structure deposition date
2017-06-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
5
Peptide accession
Q9UEF7
Residue number A
521
Residue number B
963
Peptide name
Klotho

Ligandability

Cysteine 521 of Klotho

Cysteine 963 of Klotho

A redox-regulated disulphide may form within Klotho between cysteines 910 and 970. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5w21
Structure name
crystal structure of a 1:1:1 fgf23-fgfr1c-aklotho ternary complex
Structure deposition date
2017-06-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9UEF7
Residue number A
910
Residue number B
970
Peptide name
Klotho

Ligandability

Cysteine 910 of Klotho

Cysteine 970 of Klotho

A redox-regulated disulphide may form within Klotho between cysteines 521 and 973. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5w21
Structure name
crystal structure of a 1:1:1 fgf23-fgfr1c-aklotho ternary complex
Structure deposition date
2017-06-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UEF7
Residue number A
521
Residue number B
973
Peptide name
Klotho

Ligandability

Cysteine 521 of Klotho

Cysteine 973 of Klotho

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