Protein-arginine deiminase type-1
Intramolecular
Cysteine 309 and cysteine 339
Cysteine 610 and cysteine 611
Cysteine 498 and cysteine 611
Cysteine 498 and cysteine 610
Cysteine 187 and cysteine 215
5hp5 B 309 B 339
A redox-regulated disulphide may form within Protein-arginine deiminase type-1 between cysteines 309 and 339.
Details
Redox score ?
71
PDB code
5hp5
Structure name
srtucture of human peptidylarginine deiminase type i (pad1)
Structure deposition date
2016-01-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
80
Peptide accession
Q9ULC6
Residue number A
309
Residue number B
339
Peptide name
Protein-arginine deiminase type-1
Ligandability
Cysteine 309 of Protein-arginine deiminase type-1
Cysteine 339 of Protein-arginine deiminase type-1
5hp5 B 610 B 611
A redox-regulated disulphide may form within Protein-arginine deiminase type-1 between cysteines 610 and 611. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
5hp5
Structure name
srtucture of human peptidylarginine deiminase type i (pad1)
Structure deposition date
2016-01-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
80
Peptide accession
Q9ULC6
Residue number A
610
Residue number B
611
Peptide name
Protein-arginine deiminase type-1
Ligandability
Cysteine 610 of Protein-arginine deiminase type-1
Cysteine 611 of Protein-arginine deiminase type-1
5hp5 A 498 A 611
A redox-regulated disulphide may form within Protein-arginine deiminase type-1 between cysteines 498 and 611. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5hp5
Structure name
srtucture of human peptidylarginine deiminase type i (pad1)
Structure deposition date
2016-01-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
88
Peptide accession
Q9ULC6
Residue number A
498
Residue number B
611
Peptide name
Protein-arginine deiminase type-1
Ligandability
Cysteine 498 of Protein-arginine deiminase type-1
Cysteine 611 of Protein-arginine deiminase type-1
5hp5 A 498 A 610
A redox-regulated disulphide may form within Protein-arginine deiminase type-1 between cysteines 498 and 610. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5hp5
Structure name
srtucture of human peptidylarginine deiminase type i (pad1)
Structure deposition date
2016-01-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
91
Peptide accession
Q9ULC6
Residue number A
498
Residue number B
610
Peptide name
Protein-arginine deiminase type-1
Ligandability
Cysteine 498 of Protein-arginine deiminase type-1
Cysteine 610 of Protein-arginine deiminase type-1
5hp5 B 187 B 215
A redox-regulated disulphide may form within Protein-arginine deiminase type-1 between cysteines 187 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
5hp5
Structure name
srtucture of human peptidylarginine deiminase type i (pad1)
Structure deposition date
2016-01-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
79
Peptide accession
Q9ULC6
Residue number A
187
Residue number B
215
Peptide name
Protein-arginine deiminase type-1
Ligandability
Cysteine 187 of Protein-arginine deiminase type-1
Cysteine 215 of Protein-arginine deiminase type-1
If this tool was useful for finding a disulphide, please cite: