ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Mannose-binding protein C

Intramolecular
Cysteine 155 and cysteine 244
Cysteine 222 and cysteine 236
A redox-regulated disulphide may form within Mannose-binding protein C between cysteines 155 and 244 (135 and 224 respectively in this structure).

Details

Redox score ?
82
PDB code
1hup
Structure name
human mannose binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil
Structure deposition date
1994-09-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P11226
Residue number A
155
Residue number B
244
Peptide name
Mannose-binding protein C

Ligandability

Cysteine 155 of Mannose-binding protein C

Cysteine 244 of Mannose-binding protein C

A redox-regulated disulphide may form within Mannose-binding protein C between cysteines 222 and 236 (202 and 216 respectively in this structure).

Details

Redox score ?
81
PDB code
1hup
Structure name
human mannose binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil
Structure deposition date
1994-09-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P11226
Residue number A
222
Residue number B
236
Peptide name
Mannose-binding protein C

Ligandability

Cysteine 222 of Mannose-binding protein C

Cysteine 236 of Mannose-binding protein C

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