Cathepsin F
Intramolecular
Cysteine 292 and cysteine 333
Cysteine 326 and cysteine 366
Cysteine 424 and cysteine 472
Cysteine 292 and cysteine 295
1m6d A 22 A 63
A redox-regulated disulphide may form within Cathepsin F between cysteines 292 and 333 (22 and 63 respectively in this structure).
Details
Redox score ?
86
PDB code
1m6d
Structure name
crystal structure of human cathepsin f
Structure deposition date
2002-07-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UBX1
Residue number A
292
Residue number B
333
Peptide name
Cathepsin F
Ligandability
Cysteine 292 of Cathepsin F
Cysteine 333 of Cathepsin F
1m6d A 56 A 95
A redox-regulated disulphide may form within Cathepsin F between cysteines 326 and 366 (56 and 95 respectively in this structure).
Details
Redox score ?
85
PDB code
1m6d
Structure name
crystal structure of human cathepsin f
Structure deposition date
2002-07-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UBX1
Residue number A
326
Residue number B
366
Peptide name
Cathepsin F
Ligandability
Cysteine 326 of Cathepsin F
Cysteine 366 of Cathepsin F
1m6d A 153 A 200
A redox-regulated disulphide may form within Cathepsin F between cysteines 424 and 472 (153 and 200 respectively in this structure).
Details
Redox score ?
84
PDB code
1m6d
Structure name
crystal structure of human cathepsin f
Structure deposition date
2002-07-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UBX1
Residue number A
424
Residue number B
472
Peptide name
Cathepsin F
Ligandability
Cysteine 424 of Cathepsin F
Cysteine 472 of Cathepsin F
1m6d B 22 B 25
A redox-regulated disulphide may form within Cathepsin F between cysteines 292 and 295 (22 and 25 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
1m6d
Structure name
crystal structure of human cathepsin f
Structure deposition date
2002-07-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9UBX1
Residue number A
292
Residue number B
295
Peptide name
Cathepsin F
Ligandability
Cysteine 292 of Cathepsin F
Cysteine 295 of Cathepsin F
If this tool was useful for finding a disulphide, please cite: