Fascin
Intramolecular
Cysteine 61 and cysteine 89 L
Cysteine 80 and cysteine 89 L
Cysteine 260 and cysteine 305
1dfc A 1061 A 1089
A redox-regulated disulphide may form within Fascin between cysteines 61 and 89 (1061 and 1089 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
1dfc
Structure name
crystal structure of human fascin, an actin-crosslinking protein
Structure deposition date
1999-11-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
43
Peptide accession
Q16658
Residue number A
61
Residue number B
89
Peptide name
Fascin
Ligandability
Cysteine 61 of Fascin
Cysteine 89 of Fascin
6i16 A 80 A 89
A redox-regulated disulphide may form within Fascin between cysteines 80 and 89. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6i16
Structure name
crystal structure of fascin in complex with compound 15
Structure deposition date
2018-10-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
58
Peptide accession
Q16658
Residue number A
80
Residue number B
89
Peptide name
Fascin
Ligandability
Cysteine 80 of Fascin
Cysteine 89 of Fascin
6i16 A 260 A 305
A redox-regulated disulphide may form within Fascin between cysteines 260 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6i16
Structure name
crystal structure of fascin in complex with compound 15
Structure deposition date
2018-10-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
96
Peptide accession
Q16658
Residue number A
260
Residue number B
305
Peptide name
Fascin
Ligandability
Cysteine 260 of Fascin
Cysteine 305 of Fascin
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