Dihydropyrimidinase-related protein 5
Intramolecular
Cysteine 125 and cysteine 454
Cysteine 181 and cysteine 241
Cysteine 126 and cysteine 454
Cysteine 125 and cysteine 126
Cysteine 126 and cysteine 462
4b92 A 125 A 454
A redox-regulated disulphide may form within Dihydropyrimidinase-related protein 5 between cysteines 125 and 454.
Details
Redox score ?
76
PDB code
4b92
Structure name
crystal structure of truncated human crmp-5 soaked with zn
Structure deposition date
2012-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
62
Peptide accession
Q9BPU6
Residue number A
125
Residue number B
454
Peptide name
Dihydropyrimidinase-related protein 5
Ligandability
Cysteine 125 of Dihydropyrimidinase-related protein 5
Cysteine 454 of Dihydropyrimidinase-related protein 5
4b91 A 181 A 241
A redox-regulated disulphide may form within Dihydropyrimidinase-related protein 5 between cysteines 181 and 241. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
4b91
Structure name
crystal structure of truncated human crmp-5
Structure deposition date
2012-08-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
Q9BPU6
Residue number A
181
Residue number B
241
Peptide name
Dihydropyrimidinase-related protein 5
Ligandability
Cysteine 181 of Dihydropyrimidinase-related protein 5
Cysteine 241 of Dihydropyrimidinase-related protein 5
4b91 A 126 A 454
A redox-regulated disulphide may form within Dihydropyrimidinase-related protein 5 between cysteines 126 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
4b91
Structure name
crystal structure of truncated human crmp-5
Structure deposition date
2012-08-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
7
% buried
78
Peptide accession
Q9BPU6
Residue number A
126
Residue number B
454
Peptide name
Dihydropyrimidinase-related protein 5
Ligandability
Cysteine 126 of Dihydropyrimidinase-related protein 5
Cysteine 454 of Dihydropyrimidinase-related protein 5
4b91 A 125 A 126
A redox-regulated disulphide may form within Dihydropyrimidinase-related protein 5 between cysteines 125 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4b91
Structure name
crystal structure of truncated human crmp-5
Structure deposition date
2012-08-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
14
% buried
82
Peptide accession
Q9BPU6
Residue number A
125
Residue number B
126
Peptide name
Dihydropyrimidinase-related protein 5
Ligandability
Cysteine 125 of Dihydropyrimidinase-related protein 5
Cysteine 126 of Dihydropyrimidinase-related protein 5
4b91 B 126 B 462
A redox-regulated disulphide may form within Dihydropyrimidinase-related protein 5 between cysteines 126 and 462. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
4b91
Structure name
crystal structure of truncated human crmp-5
Structure deposition date
2012-08-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
92
Peptide accession
Q9BPU6
Residue number A
126
Residue number B
462
Peptide name
Dihydropyrimidinase-related protein 5
Ligandability
Cysteine 126 of Dihydropyrimidinase-related protein 5
Cysteine 462 of Dihydropyrimidinase-related protein 5
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