ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ceruloplasmin

Intramolecular
Cysteine 276 and cysteine 357
Cysteine 637 and cysteine 718
Cysteine 534 and cysteine 560
Cysteine 174 and cysteine 200
Cysteine 874 and cysteine 900
A redox-regulated disulphide may form within Ceruloplasmin between cysteines 276 and 357 (257 and 338 respectively in this structure).

Details

Redox score ?
87
PDB code
1kcw
Structure name
x-ray crystal structure of human ceruloplasmin at 3
Structure deposition date
1996-09-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00450
Residue number A
276
Residue number B
357
Peptide name
Ceruloplasmin

Ligandability

Cysteine 276 of Ceruloplasmin

Cysteine 357 of Ceruloplasmin

A redox-regulated disulphide may form within Ceruloplasmin between cysteines 637 and 718 (618 and 699 respectively in this structure).

Details

Redox score ?
82
PDB code
4ejx
Structure name
structure of ceruloplasmin-myeloperoxidase complex
Structure deposition date
2012-04-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00450
Residue number A
637
Residue number B
718
Peptide name
Ceruloplasmin

Ligandability

Cysteine 637 of Ceruloplasmin

Cysteine 718 of Ceruloplasmin

A redox-regulated disulphide may form within Ceruloplasmin between cysteines 534 and 560 (515 and 541 respectively in this structure).

Details

Redox score ?
81
PDB code
1kcw
Structure name
x-ray crystal structure of human ceruloplasmin at 3
Structure deposition date
1996-09-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00450
Residue number A
534
Residue number B
560
Peptide name
Ceruloplasmin

Ligandability

Cysteine 534 of Ceruloplasmin

Cysteine 560 of Ceruloplasmin

A redox-regulated disulphide may form within Ceruloplasmin between cysteines 174 and 200 (155 and 181 respectively in this structure).

Details

Redox score ?
78
PDB code
1kcw
Structure name
x-ray crystal structure of human ceruloplasmin at 3
Structure deposition date
1996-09-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00450
Residue number A
174
Residue number B
200
Peptide name
Ceruloplasmin

Ligandability

Cysteine 174 of Ceruloplasmin

Cysteine 200 of Ceruloplasmin

A redox-regulated disulphide may form within Ceruloplasmin between cysteines 874 and 900 (855 and 881 respectively in this structure).

Details

Redox score ?
78
PDB code
4enz
Structure name
structure of human ceruloplasmin at 2
Structure deposition date
2012-04-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00450
Residue number A
874
Residue number B
900
Peptide name
Ceruloplasmin

Ligandability

Cysteine 874 of Ceruloplasmin

Cysteine 900 of Ceruloplasmin

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